Academic literature on the topic 'Ribosome biogensis'

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Journal articles on the topic "Ribosome biogensis"

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Moraleva, Anastasia A., Alexander S. Deryabin, Yury P. Rubtsov, Maria P. Rubtsova, and Olga A. Dontsova. "Eukaryotic Ribosome Biogenesis: The 40S Subunit." Acta Naturae 14, no. 1 (May 10, 2022): 14–30. http://dx.doi.org/10.32607/actanaturae.11540.

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The formation of eukaryotic ribosomes is a sequential process of ribosomal precursors maturation in the nucleolus, nucleoplasm, and cytoplasm. Hundreds of ribosomal biogenesis factors ensure the accurate processing and formation of the ribosomal RNAs tertiary structure, and they interact with ribosomal proteins. Most of what we know about the ribosome assembly has been derived from yeast cell studies, and the mechanisms of ribosome biogenesis in eukaryotes are considered quite conservative. Although the main stages of ribosome biogenesis are similar across different groups of eukaryotes, this process in humans is much more complicated owing to the larger size of the ribosomes and pre-ribosomes and the emergence of regulatory pathways that affect their assembly and function. Many of the factors involved in the biogenesis of human ribosomes have been identified using genome-wide screening based on RNA interference. This review addresses the key aspects of yeast and human ribosome biogenesis, using the 40S subunit as an example. The mechanisms underlying these differences are still not well understood, because, unlike yeast, there are no effective methods for characterizing pre-ribosomal complexes in humans. Understanding the mechanisms of human ribosome assembly would have an incidence on a growing number of genetic diseases (ribosomopathies) caused by mutations in the genes encoding ribosomal proteins and ribosome biogenesis factors. In addition, there is evidence that ribosome assembly is regulated by oncogenic signaling pathways, and that defects in the ribosome biogenesis are linked to the activation of tumor suppressors.
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Moraleva, Anastasia A., Alexander S. Deryabin, Yury P. Rubtsov, Maria P. Rubtsova, and Olga A. Dontsova. "Eukaryotic Ribosome Biogenesis: The 60S Subunit." Acta Naturae 14, no. 2 (July 21, 2022): 39–49. http://dx.doi.org/10.32607/actanaturae.11541.

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Ribosome biogenesis is consecutive coordinated maturation of ribosomal precursors in the nucleolus, nucleoplasm, and cytoplasm. The formation of mature ribosomal subunits involves hundreds of ribosomal biogenesis factors that ensure ribosomal RNA processing, tertiary structure, and interaction with ribosomal proteins. Although the main features and stages of ribosome biogenesis are conservative among different groups of eukaryotes, this process in human cells has become more complicated due to the larger size of the ribosomes and pre-ribosomes and intricate regulatory pathways affecting their assembly and function. Many of the factors involved in the biogenesis of human ribosomes have been identified using genome-wide screening based on RNA interference. A previous part of this review summarized recent data on the processing of the primary rRNA transcript and compared the maturation of the small 40S subunit in yeast and human cells. This part of the review focuses on the biogenesis of the large 60S subunit of eukaryotic ribosomes.
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Sulima, Sergey, Kim Kampen, and Kim De Keersmaecker. "Cancer Biogenesis in Ribosomopathies." Cells 8, no. 3 (March 11, 2019): 229. http://dx.doi.org/10.3390/cells8030229.

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Ribosomopathies are congenital diseases with defects in ribosome assembly and are characterized by elevated cancer risks. Additionally, somatic mutations in ribosomal proteins have recently been linked to a variety of cancers. Despite a clear correlation between ribosome defects and cancer, the molecular mechanisms by which these defects promote tumorigenesis are unclear. In this review, we focus on the emerging mechanisms that link ribosomal defects in ribosomopathies to cancer progression. This includes functional “onco-specialization” of mutant ribosomes, extra-ribosomal consequences of mutations in ribosomal proteins and ribosome assembly factors, and effects of ribosomal mutations on cellular stress and metabolism. We integrate some of these recent findings in a single model that can partially explain the paradoxical transition from hypo- to hyperproliferation phenotypes, as observed in ribosomopathies. Finally, we discuss the current and potential strategies, and the associated challenges for therapeutic intervention in ribosome-mutant diseases.
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Konikkat, Salini, and John L. Woolford,. "Principles of 60S ribosomal subunit assembly emerging from recent studies in yeast." Biochemical Journal 474, no. 2 (January 6, 2017): 195–214. http://dx.doi.org/10.1042/bcj20160516.

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Ribosome biogenesis requires the intertwined processes of folding, modification, and processing of ribosomal RNA, together with binding of ribosomal proteins. In eukaryotic cells, ribosome assembly begins in the nucleolus, continues in the nucleoplasm, and is not completed until after nascent particles are exported to the cytoplasm. The efficiency and fidelity of ribosome biogenesis are facilitated by >200 assembly factors and ∼76 different small nucleolar RNAs. The pathway is driven forward by numerous remodeling events to rearrange the ribonucleoprotein architecture of pre-ribosomes. Here, we describe principles of ribosome assembly that have emerged from recent studies of biogenesis of the large ribosomal subunit in the yeast Saccharomyces cerevisiae. We describe tools that have empowered investigations of ribosome biogenesis, and then summarize recent discoveries about each of the consecutive steps of subunit assembly.
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Pecoraro, Annalisa, Martina Pagano, Giulia Russo, and Annapina Russo. "Ribosome Biogenesis and Cancer: Overview on Ribosomal Proteins." International Journal of Molecular Sciences 22, no. 11 (May 23, 2021): 5496. http://dx.doi.org/10.3390/ijms22115496.

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Cytosolic ribosomes (cytoribosomes) are macromolecular ribonucleoprotein complexes that are assembled from ribosomal RNA and ribosomal proteins, which are essential for protein biosynthesis. Mitochondrial ribosomes (mitoribosomes) perform translation of the proteins essential for the oxidative phosphorylation system. The biogenesis of cytoribosomes and mitoribosomes includes ribosomal RNA processing, modification and binding to ribosomal proteins and is assisted by numerous biogenesis factors. This is a major energy-consuming process in the cell and, therefore, is highly coordinated and sensitive to several cellular stressors. In mitochondria, the regulation of mitoribosome biogenesis is essential for cellular respiration, a process linked to cell growth and proliferation. This review briefly overviews the key stages of cytosolic and mitochondrial ribosome biogenesis; summarizes the main steps of ribosome biogenesis alterations occurring during tumorigenesis, highlighting the changes in the expression level of cytosolic ribosomal proteins (CRPs) and mitochondrial ribosomal proteins (MRPs) in different types of tumors; focuses on the currently available information regarding the extra-ribosomal functions of CRPs and MRPs correlated to cancer; and discusses the role of CRPs and MRPs as biomarkers and/or molecular targets in cancer treatment.
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Lavdovskaia, Elena, Kärt Denks, Franziska Nadler, Emely Steube, Andreas Linden, Henning Urlaub, Marina V. Rodnina, and Ricarda Richter-Dennerlein. "Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes." Nucleic Acids Research 48, no. 22 (December 2, 2020): 12929–42. http://dx.doi.org/10.1093/nar/gkaa1132.

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Abstract Translation and ribosome biogenesis in mitochondria require auxiliary factors that ensure rapid and accurate synthesis of mitochondrial proteins. Defects in translation are associated with oxidative phosphorylation deficiency and cause severe human diseases, but the exact roles of mitochondrial translation-associated factors are not known. Here we identify the functions of GTPBP6, a homolog of the bacterial ribosome-recycling factor HflX, in human mitochondria. Similarly to HflX, GTPBP6 facilitates the dissociation of ribosomes in vitro and in vivo. In contrast to HflX, GTPBP6 is also required for the assembly of mitochondrial ribosomes. GTPBP6 ablation leads to accumulation of late assembly intermediate(s) of the large ribosomal subunit containing ribosome biogenesis factors MTERF4, NSUN4, MALSU1 and the GTPases GTPBP5, GTPBP7 and GTPBP10. Our data show that GTPBP6 has a dual function acting in ribosome recycling and biogenesis. These findings contribute to our understanding of large ribosomal subunit assembly as well as ribosome recycling pathway in mitochondria.
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Slimane, Sophie Nait, Virginie Marcel, Tanguy Fenouil, Frédéric Catez, Jean-Christophe Saurin, Philippe Bouvet, Jean-Jacques Diaz, and Hichem C. Mertani. "Ribosome Biogenesis Alterations in Colorectal Cancer." Cells 9, no. 11 (October 27, 2020): 2361. http://dx.doi.org/10.3390/cells9112361.

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Many studies have focused on understanding the regulation and functions of aberrant protein synthesis in colorectal cancer (CRC), leaving the ribosome, its main effector, relatively underappreciated in CRC. The production of functional ribosomes is initiated in the nucleolus, requires coordinated ribosomal RNA (rRNA) processing and ribosomal protein (RP) assembly, and is frequently hyperactivated to support the needs in protein synthesis essential to withstand unremitting cancer cell growth. This elevated ribosome production in cancer cells includes a strong alteration of ribosome biogenesis homeostasis that represents one of the hallmarks of cancer cells. None of the ribosome production steps escape this cancer-specific dysregulation. This review summarizes the early and late steps of ribosome biogenesis dysregulations described in CRC cell lines, intestinal organoids, CRC stem cells and mouse models, and their possible clinical implications. We highlight how this cancer-related ribosome biogenesis, both at quantitative and qualitative levels, can lead to the synthesis of ribosomes favoring the translation of mRNAs encoding hyperproliferative and survival factors. We also discuss whether cancer-related ribosome biogenesis is a mere consequence of cancer progression or is a causal factor in CRC, and how altered ribosome biogenesis pathways can represent effective targets to kill CRC cells. The association between exacerbated CRC cell growth and alteration of specific steps of ribosome biogenesis is highlighted as a key driver of tumorigenesis, providing promising perspectives for the implementation of predictive biomarkers and the development of new therapeutic drugs.
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Jovanovic, Bogdan, Lisa Schubert, Fabian Poetz, and Georg Stoecklin. "Tagging of RPS9 as a tool for ribosome purification and identification of ribosome-associated proteins." Archives of Biological Sciences, no. 00 (2020): 57. http://dx.doi.org/10.2298/abs20120557j.

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Ribosomes, the catalytic machinery required for protein synthesis, are comprised of 4 ribosomal RNAs and about 80 ribosomal proteins in mammals. Ribosomes further interact with numerous associated factors that regulate their biogenesis and function. As mutations of ribosomal proteins and ribosome associated proteins cause many diseases, it is important to develop tools by which ribosomes can be purified efficiently and with high specificity. Here, we designed a method to purify ribosomes from human cell lines by C-terminally tagging human RPS9, a protein of the small ribosomal subunit. The tag consists of a flag peptide and a streptavidin-binding peptide (SBP) separated by the tobacco etch virus (TEV) protease cleavage site. We demonstrate that RPS9-Flag-TEV-SBP (FTS) is efficiently incorporated into the ribosome without interfering with regular protein synthesis. Using HeLa-GFP-G3BP1 cells stably expressing RPS9-FTS or, as a negative control, mCherry-FTS, we show that complete ribosomes as well as numerous ribosome-associated proteins are efficiently and specifically purified following pull-down of RPS9-FTS using streptavidin beads. This tool will be helpful for the characterization of human ribosome heterogeneity, post-translational modifications of ribosomal proteins, and changes in ribosome-associated factors after exposing human cells to different stimuli and conditions.
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Temaj, Gazmend, Silvia Chichiarelli, Margherita Eufemi, Fabio Altieri, Rifat Hadziselimovic, Ammad Ahmad Farooqi, Ilhan Yaylim, and Luciano Saso. "Ribosome-Directed Therapies in Cancer." Biomedicines 10, no. 9 (August 26, 2022): 2088. http://dx.doi.org/10.3390/biomedicines10092088.

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The human ribosomes are the cellular machines that participate in protein synthesis, which is deeply affected during cancer transformation by different oncoproteins and is shown to provide cancer cell proliferation and therefore biomass. Cancer diseases are associated with an increase in ribosome biogenesis and mutation of ribosomal proteins. The ribosome represents an attractive anti-cancer therapy target and several strategies are used to identify specific drugs. Here we review the role of different drugs that may decrease ribosome biogenesis and cancer cell proliferation.
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Pelava, Andria, Claudia Schneider, and Nicholas J. Watkins. "The importance of ribosome production, and the 5S RNP–MDM2 pathway, in health and disease." Biochemical Society Transactions 44, no. 4 (August 15, 2016): 1086–90. http://dx.doi.org/10.1042/bst20160106.

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Ribosomes are abundant, large RNA–protein complexes that are the source of all protein synthesis in the cell. The production of ribosomes is an extremely energetically expensive cellular process that has long been linked to human health and disease. More recently, it has been shown that ribosome biogenesis is intimately linked to multiple cellular signalling pathways and that defects in ribosome production can lead to a wide variety of human diseases. Furthermore, changes in ribosome production in response to nutrient levels in the diet lead to metabolic re-programming of the liver. Reduced or abnormal ribosome production in response to cellular stress or mutations in genes encoding factors critical for ribosome biogenesis causes the activation of the tumour suppressor p53, which leads to re-programming of cellular transcription. The ribosomal assembly intermediate 5S RNP (ribonucleoprotein particle), containing RPL5, RPL11 and the 5S rRNA, accumulates when ribosome biogenesis is blocked. The excess 5S RNP binds to murine double minute 2 (MDM2), the main p53-suppressor in the cell, inhibiting its function and leading to p53 activation. Here, we discuss the involvement of ribosome biogenesis in the homoeostasis of p53 in the cell and in human health and disease.
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Dissertations / Theses on the topic "Ribosome biogensis"

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Dator, Romel P. "Characterization of Ribosomes and Ribosome Assembly Complexes by Mass Spectrometry." University of Cincinnati / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1382373082.

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Burlacu, Elena. "Probing ribosomal RNA structural rearrangements : a time lapse of ribosome assembly dynamics." Thesis, University of Edinburgh, 2016. http://hdl.handle.net/1842/17072.

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Ribosome synthesis is a very complex and energy consuming process in which pre-ribosomal RNA (pre-rRNA) processing and folding events, sequential binding of ribosomal proteins and the input of approximately 200 trans-acting ribosome assembly factors need to be tightly coordinated. In the yeast Saccharomyces cerevisiae, ribosome assembly starts in the nucleolus with the formation of a very large 90S-sized complex. This ~2.2MDa pre-ribosomal complex is subsequently processed into the 40S and 60S assembly intermediates (pre-40S and pre-60S), which subsequently mature largely independently. Although we have a fairly complete picture of the protein composition of these pre-ribosomes, still very little is known about the rRNA structural rearrangements that take place during the assembly of the 40S and 60S subunits and the role of the ribosome assembly factors in this process. To address this, the Granneman lab developed a method called ChemModSeq, which made it possible to generate nucleotide resolution maps of RNA flexibility in ribonucleoprotein complexes by combining SHAPE chemical probing, high-throughput sequencing and statistical modelling. By applying ChemModSeq to ribosome assembly intermediates, we were able to obtain nucleotide resolution insights into rRNA structural rearrangements during late (cytoplasmic) stages of 40S assembly and for the early (nucleolar) stages of 60S assembly. The results revealed structurally distinct cytoplasmic pre-40S particles in which rRNA restructuring events coincide with the hierarchical dissociation of assembly factors. These rearrangements are required to trigger stable incorporation of a number of ribosomal proteins and the completion of the head domain. Rps17, one of the ribosomal proteins that fully assembled into pre-40S complexes only at a later assembly stage, was further characterized. Surprisingly, my ChemModSeq analyses of nucleolar pre-60S complexes indicated that most of the rRNA folding steps take place at a very specific stage of maturation. One of the most striking observations was the stabilization of 5.8S pre-rRNA region, which coincided with the dissociation of the assembly factor Rrp5 and stable incorporation of a number of ribosomal proteins.
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Gartmann, Marco. "Structural characterization of ribosomal complexes involved in ribosome biogenesis and protein folding." Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-120476.

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Zakari, Musinu. "The SMC loader Scc2 promotes ncRNA biogenesis and translational fidelity in Saccharomyces cerevisiae." Thesis, Paris 6, 2015. http://www.theses.fr/2015PA066148/document.

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Le complexe Scc2-Scc4 est essentiel pour l’association du complexe cohésine sur l’ADN. Les proteines Cohésine génèrent la cohésion entre les chromatides sœurs, ce qui est essentiel pour la ségrégation des chromosomes. Scc2 (également connu sous le nom NIPBL) est muté chez les patients atteints du syndrome de Cornelia de Lange, une maladie multi-organique caractérisée par des anomalies du développement du visage, de la developpement mental cardiaque et du tractus gastro-intestinal. Comment les mutations localisées au niveau du gène codant pour la proteine Scc2 conduisent à des anomalies du développement chez les patients n’a pas encore été élucidé. Une des hypothèses est que la liaison de Scc2 / cohésine à différentes régions du génome a une incidence sur la transcription. Chez la levure de bière, il a été montre que Scc2 se lie aux genes transcrits par l'ARN Pol III (les ARNt et spliceosomals) , ainsi qu‘aux gènes transcrits par l'ARN Pol II codant pour des petits ARN nucléolaires et nucléaires (snARN et snoARNs ) et des gènes de protéines ribosomiques. Nous rapportons ici que Scc2 est important pour l'expression de ces gènes. Scc2 et le régulateur transcriptionnel Paf1 collaborent pour promouvoir la production de Box H / ACA snoARNs qui guident la pseudouridylation des ARN y compris l'ARN ribosomal. Une mutation de Scc2 a été associée à des défauts dans la production d'ARN ribosomal, la biogenèse des ribosomes, et del’épissage. Alors que le mutant Scc2 n'a pas de défaut général de la synthèse protéique, il montre un déphasage accrue et une réduction de l’utilisation du site interne d'entrée ribosomale (IRES)/ coiffe-indépendante. Ces résultats suggèrent que Scc2 favorise normalement un programme d'expression génétique qui prend en charge la fidélité de la traduction. Nous émettons l'hypothèse que le dysfonctionnement de traduction peut contribuer au syndrome de Cornelia de Lange, qui est causé par des mutations dans Scc2
The Scc2-Scc4 complex is essential for loading the cohesin complex onto DNA. Cohesin generates cohesion between sister chromatids, which is critical for chromosome segregation. Scc2 (also known as NIPBL) is mutated in patients with Cornelia de Lange syndrome, a multi-organ disease characterized by developmental defects in head, limb, cognition, heart, and the gastrointestinal tract. How mutations in Scc2 lead to developmental defects in patients is yet to be elucidated. One hypothesis is that the binding of Scc2/cohesin to different regions of the genome will affect transcription. In budding yeast, Scc2 has been shown to bind to RNA Pol III transcribed genes (tRNAs, and spliceosomal), as well as RNA Pol II-transcribed genes encoding small nuclear and nucleolar RNAs (snRNAs and snoRNAs) and ribosomal protein genes. Here, we report that Scc2 is important for gene expression. Scc2 and the transcriptional regulator Paf1 collaborate to promote the production of Box H/ACA snoRNAs which guide pseudouridylation of RNAs including ribosomal RNA. Mutation of Scc2 was associated with defects in the production of ribosomal RNA, ribosome biogenesis, and splicing. While the scc2 mutant does not have a general defect in protein synthesis, it shows increased frameshifting and reduced internal ribosomal entry site (IRES) usage/cap-independent translation. These findings suggest Scc2 normally promotes a gene expression program that supports translational fidelity. We hypothesize that translational dysfunction may contribute to the human disorder Cornelia de Lange syndrome, which is caused by mutations in Scc2
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Ramesh, Madhumitha. "Analysis of Ribosome Biogenesis from Three Standpoints: Investigating the Roles of Ribosomal RNA, Ribosomal Proteins and Assembly Factors." Research Showcase @ CMU, 2016. http://repository.cmu.edu/dissertations/609.

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Ribosomes are ubiquitous and abundant molecular machines composed of ribosomal RNA (rRNA) and ribosomal proteins (r-proteins). They play a central role in the cell by translating the genetic code in mRNA to form polypeptides. Because of their large size and the complexity of molecular interactions within ribosomes, we do not still fully understand how they are synthesized in the cell. Yet, a thorough knowledge of ribosome biogenesis is crucial to understand cellular homeostasis and various disease states including ribosomopathies and cancer. In addition, ribosomes serve as an interesting paradigm to understand the principles that dictate the formation and function of the many different ribonucleoprotein particles that play vital roles in the cell. In addition to the rRNA and r-protein components, trans-acting assembly factors play indispensable roles in synthesizing functional ribosomes. Fundamentally, ribosome biogenesis is driven by a network of molecular interactions that evolve in time and space, as assembly progresses from the nucleolus to the cytoplasm. We sought to gain a deeper understanding of ribosome biogenesis in Saccharomyces cerevisiae by investigating the molecular interactions that drive ribosome assembly. Recent structural studies have revealed a number of such molecular interactions at high resolution. Based on these, our investigation was carried out from the perspectives of all three players that are involved in constructing ribosomes, with a specific emphasis on eukaryote-specific elements of rRNAs and r-proteins. From the standpoint of rRNA, we performed the first systematic study to investigate the potential functions of nearly all of the eukaryotic rRNA expansion segments in the yeast large ribosomal subunit. We showed that most of them are indispensable and play vital roles in ribosome biogenesis. Based on the steps of ribosome biogenesis in which each of them participates, we showed that there is neighborhood-specific functional clustering of rRNA and r-protein interactions that drive ribosome assembly. Further, we found evidence for possible functional co-evolution of eukaryotic rRNA and eukaryote-specific elements of r-protein. From the standpoint of r-protein, we used rpL5 as a paradigm for constantly evolving molecular interactions as assembly progresses. Apart from recapitulating Diamond-Blackfan anemia missense mutations in yeast, we characterized interactions formed by specific regions of rpL5 and propose that these interactions potentially govern the loading of 5S RNP en bloc to the nascent large ribosomal subunit, to ensure proper rotation of the 5S RNP during biogenesis, and to further recruit proteins necessary for the test drive of subunits in the cytoplasm. From the standpoint of assembly factors, we analyzed a so-called group of ITS2 cluster proteins, Nop15, Cic1 and Rlp7 and identified the extensive protein-protein interactions and analyzed protein-RNA interactions that they make. Using our data, we were able to localize Rlp7 to the ITS2 spacer in the pre-rRNA and to identify potential mechanisms for their function. Having identified a network of molecular interactions, we suggest that these proteins orchestrate proper folding of rRNA through this network, and stabilize and facilitate the early steps of assembly. Further, based on their location in the preribosome, these factors might serve to ensure proper progression of early steps of assembly to enable subsequent processing of the ITS2 spacer in the middle steps, possibly by recruiting the ATPase Has1. Thus, we have investigated early nucleolar and late nuclear steps of ribosome assembly in the light of molecular interactions formed by rRNA, r-protein and assembly factors that participate in eukaryotic ribosome assembly. Lessons that emerged from this study and tools developed in the process provide a starting point for further investigations pertaining to the roles of eukaryote-specific segments of molecules that participate in ribosome biogenesis, and serve as a paradigm for how a dynamic network of molecular interactions can drive the assembly of complex macromolecular structures.
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Therizols, Gabriel. "Rôle des ribosomes et de leur biogenèse dans la tumorigenèse et la réponse aux traitements chimiothérapeutiques." Thesis, Lyon 1, 2014. http://www.theses.fr/2014LYO10083/document.

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Les cellules cancéreuses produisent une grande quantité de ribosomes afin de synthétiser les protéines nécessaires à leur prolifération rapide. Les mécanismes qui conduisent à cette augmentation de la production de ribosome ne sont que partiellement compris, mais ils semblent intimement liés à l'acquisition du phénotype tumoral. De plus, une nouvelle théorie propose que les ribosomes ne sont pas des effecteurs neutres de la traduction, mais qu'ils jouent un rôle direct dans la régulation de l'expression génique. Cette théorie se base sur l'observation que la composition des ribosomes est hétérogène en fonction des types cellulaires et des conditions environnementales. Dans ce contexte, j'ai étudié les liens entre les altérations des signaux qui contrôlent la biogenèse des ribosomes, tant au niveau quantitatif que qualitatif, et le développement du phénotype tumoral. Ce manuscrit rapporte trois études effectuées au cours de mon travail de thèse. Ces études ont permis d'identifier : i) un nouveau régulateur de la quantité de ribosomes, la LN-Nétrine-1 et ii) des modifications de la composition et de la fonction des ribosomes induites par des altérations génétiques (perte d'activité de p53) et par l'utilisation d'une molécule chimiothérapeutique, le 5- Fluorouracile. Ces perturbations de la quantité et de la fonction des ribosomes modifient le contrôle de la traduction des cellules et la croissance, la prolifération et la survie cellulaire. Il ressort de ces résultats que les ribosomes sont des éléments qui participent au contrôle de l'expression génique et qui jouent un rôle dans la pathologie cancéreuse et la réponse au traitement chimiothérapeutique
Cancer cells produce large amounts of ribosomes to synthesize the proteins required for their rapid proliferation. The mechanisms leading to this increase in ribosome production are only partly understood, but they are related to the acquisition of the tumor phenotype. In addition, a new theory proposes that ribosomes are not neutral effectors of translation, but have a direct role in the regulation of gene expression. This theory is based on the observation that ribosome composition is heterogeneous in different cell types and according to environmental conditions. In this context, I have analyzed the relationships between changes in signals that control ribosome biogenesis, both quantitatively and qualitatively, and the development of the tumor phenotype. This manuscript reports three studies made during this PhD program. These studies identified: i) a novel regulator of the amount of ribosomes, the LN-Netrin-1 and ii) changes in the ribosome composition and function induced by genetic alterations (loss of activity of p53) and by the use of a chemotherapeutic molecule, the 5-Fluorouracil. These perturbations of the amount and the function of ribosomes modify the translation control and cell growth, cell proliferation and cell survival. From these results it can be conclude that ribosomes are elements involved in the regulation of gene expression and play a role in cancer pathology and response to chemotherapy
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G, C. Keshav. "Investigation of the Role of Bacterial Ribosomal RNA Methyltransferase Enzyme RsmC in Ribosome Biogenesis." Kent State University / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=kent1621868567263046.

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Bouffard, Stéphanie. "Study of ribosome biogenesis factors in zebrafish neural progenitors." Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS228/document.

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Alors que la biogénèse des ribosomes a étéconsidérée comme un mécanisme ubiquiste, lesétapes de ce processus ont récemment étédémontrées comme étant tissu-spécifiques. Letoit optique (OT) du poisson-zèbre est un modèleapproprié pour étudier la prolifération cellulairepuisque les cellules à différents états dedifférenciation se trouvent dans des domainesséparés.Au cours de mon doctorat, j'ai examiné si lesgènes de la biogenèse des ribosomes peuventavoir des rôles spécifiques dans les cellulesprogénitrices neuroépithéliales (CPNe). Profitantd'une analyse transcriptomique antérieure, j'aid'abord examiné les nouveaux candidatsaccumulés dans les CPNe. J'ai décidé de meconcentrer sur proliferation-associated 2G4(pa2G4/ebp1) qui est exprimé de manièrepréférentielle dans les CPNe.Ce gène favorise ou réprime la proliférationcellulaire dans des organismes normaux oupendant la tumorigénèse. J'ai conçu une stratégiepour l'expression inductible et cellule-spécifiquede ce gène.Fibrillarin (Fbl), une méthyltranférasenucléolaire est également préférentiellementexprimée dans CPNe. Ce gène joue un rôleimportant dans le cancer. J'ai montré que lesmutants fbl présentaient des défauts OTspécifiques,en lien avec une apoptose massive etune absence de différenciation neurale. J'aiégalement démontré une diminution de l'activitéde traduction des ribosomes. En outre, lesmutants fbl montrent une progression de la phaseS altérée. Nos données suggèrent que fbl estessentiel à la prolifération des progéniteursneuronaux du poisson-zèbre
While ribosome biogenesis has been consideredas an ubiquitous mechanism, steps of thisprocess have recently been shown to be tissuespecific. Zebrafish optic tectum (OT) is asuitable model to study cell proliferation sincecells at different differentiation states arespatially partitioned.During my PhD, I examined whether ribosomebiogenesis genes may have specific roles inneuroepithelial progenitor cells (NePCs).Taking advantage of a previous transcriptomicanalysis, I first screened for new candidatesaccumulated in NePCs. I decided to focus onproliferation-associated 2G4 (pa2g4/ebp1),which was expressed preferentially in NePCs.This gene promotes or represses cellproliferation in normal organisms or duringtumorigenesis. I designed a strategy for theinducible expression and cell specificexpression of this gene.Fibrillarin (Fbl), a small nucleolarmethyltransferase is also preferentiallyexpressed in NePCs. It plays an important rolein cancer. I showed that fbl mutants displayedspecific OT defects linked to a massiveapoptosis and an absence of neuraldifferentiation. I also demonstrated deficienciesin the ribosome translational activity.Additionally, fbl mutants showed impaired Sphaseprogression. Our data suggest that fbl isessential for the proliferation of zebrafishneuronal progenitors
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Deraze, Jérôme. "Epigenetic control of ribosome biogenesis homeostasis." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066342/document.

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La traduction est une activité cellulaire essentielle, réalisée par les ribosomes. Ces particules sont synthétisées dans le nucléole, ce qui nécessite l'expression coordonnée de 4 ARN ribosomaux, 80 protéines ribosomales, et plus de 200 facteurs d'assemblage. Leur biogenèse est complexe et sollicite plus de la moitié de l'énergie des cellules en prolifération. La quantité de ribosomes varie selon les conditions environnementales et métaboliques et de ce fait, leur synthèse est modulée en réponse à de nombreux stimuli. Plusieurs mécanismes coordonnent la biogenèse des ribosomes avec l'homéostasie cellulaire. L'un d'eux est la capacité des protéines ribosomiques à réguler l'expression des gènes à plusieurs niveaux. Ces fonctions effectuées hors du ribosome sont dites extraribosomales. Notre équipe a mis en évidence l'une de ces fonctions de la protéine ribosomale uL11 chez la Drosophile. Quand sa lysine 3 est triméthylée (uL11K3me3), elle interagit avec Corto, un facteur de transcription de la famille des Enhancers de Trithorax et Polycomb. L'étude de leur fixation à la chromatine montre que ces protéines se répartissent différemment à l'échelle du génome, et que uL11K3me3 est présente au niveau de gènes actifs enrichis en composants du ribosome. Nous avons généré les premiers allèles génétiques du gène uL11 chez la Drosophile, et décrivons la stratégie de crible moléculaire employée pour leur isolation. Finalement, nous avons étudié les allèles de uL11 dont la lysine 3 est mutée. Leurs phénotypes ressemblent à ceux des mutants Minute, suggérant que le domaine N-terminal de uL11 possède une fonction essentielle, mais peut-être indépendante d'une interaction avec Corto
Translation is an essential metabolic activity carried by ribosomes. These complexes are synthetized in the nucleolus, and require the coordinated expression of 4 ribosomal RNA, 80 ribosomal proteins, and more than 200 assembly factors. Indeed, their biogenesis is complex and expensive, consuming more than half of the energy in proliferating cells. As the cellular need for ribosomes varies with environmental or metabolic conditions, their synthesis is tightly regulated in response to a number of cues. Many mechanisms ensure that the intensity of ribosome biogenesis is coupled to cell homeostasis. Such is the ability of ribosomal proteins to regulate gene expression at many levels, from translation specificity to activation or repression of transcription. Many such functions are carried off the ribosome, and are thus termed extraribosomal. Our team discovered a new extraribosomal function of ribosomal protein uL11 in Drosophila. Indeed, when trimethylated on lysine 3 (uL11K3me3), it associates with Corto, a transcription factor of the Enhancers of Trithorax and Polycomb family. By studying their genome-wide binding profile on chromatin, we show that these proteins are distributed along different patterns, and that uL11K3me3 specifically binds a subset of active genes enriched in ribosome biogenesis components. Additionally, we generated the first genetic alleles for Drosophila uL11 and describe the molecular screening method that we employed. Last, we studied the uL11 alleles that delete or replace lysine 3. We describe that their Minute-like phenotypes suggest an essential role for the N-terminal domain of uL11, though it may be independent of its association with Corto
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Nguyen, Van Long Flora. "Altérations de composition des ribosomes dans les cancers du sein : analyses de cohortes humaines et modèles cellulaires." Thesis, Lyon, 2019. http://www.theses.fr/2019LYSE1095/document.

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Les ribosomes sont responsables de la traduction des ARNm en protéines. Des modifications de la composition des ribosomes altèrent son activité de traduction et favorisent la tumorigenèse. L’identification des altérations de composition des ribosomes dans les cancers du sein pourrait être un nouveau mécanisme de tumorigenèse mammaire et ouvrir de nouvelles perspectives thérapeutiques. En effet, les cancers du sein restent la première cause de mortalité liés aux cancers chez la femme et leur hétérogénéité induit un problème thérapeutique important. Dans ce contexte, les altérations de composition des ribosomes dans les cancers du sein ont été abordées dans des cohortes humaines et dans des modèles cellulaires de l’EMT (Transition Epithélio-Mésenchymateuse), un processus impliqué dans la tumorigenèse mammaire. Ces travaux ont permis d’identifier : i) deux facteurs impliqués dans la biogenèse des ribosomes, FBL (fibrillarine) et NCL (nucléoline) dont les variations d’expression sont associées à un mauvais pronostic chez les patientes ; et ii) des variations de composition du ribosome et de son activité traductionnelle dans l’EMT. L’ensemble de ces résultats soutient l’existence d’altérations de composition des ribosomes dans les cancers du sein
Ribosomes are responsible of translating mRNAs to proteins. Alterations of ribosome composition modify its translation activity and favour tumourigenesis. Identification of ribosomes composition alterations in breast cancers might correspond to a new mechanism responsible of mammary tumourigenesis and might open up novel therapeutic approaches. Indeed breast cancers represent the first cause of women mortality due to cancers and their heterogeneity induces an important therapeutic problem.In this context, alterations of ribosomes composition were determined in human cohorts and in EMT (Epithelial to Mesenchymal Transition) cellular models, the EMT being a process involved in mammary tumourigenesis. This studies identify : (i) two factors involved in ribosome biogenesis, FBL (fibrillarin) and NCL (nucleolin) whose expression variations are associated with poor prognosis in patients and (ii) variations of ribosome composition and its translational activity in EMT. Altogether, this data support the presence of ribosomes composition alterations in breast cancers
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Books on the topic "Ribosome biogensis"

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Entian, Karl-Dieter, ed. Ribosome Biogenesis. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9.

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The nucleolus and ribosome biogenesis. Wien: Springer-Verlag, 1985.

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Hadjiolov, Asen A. The Nucleolus and Ribosome Biogenesis. Vienna: Springer Vienna, 1985. http://dx.doi.org/10.1007/978-3-7091-8742-5.

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Hadjiolov, A. A. Nucleolus and Ribosome Biogenesis. Springer, 2012.

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Ribosome Biogenesis: Methods and Protocols. Springer, 2022.

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Hadjiolov, A. A. The Nucleolus and Ribosome Biogenesis. Springer, 2011.

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Entian, Karl-Dieter. Ribosome Biogenesis: Methods and Protocols. Springer, 2022.

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Steinbauer, Robert. Regulation of ribosome biogenesis and RNA polymerase I transcription: How nutrients control the synthesis of ribosomes. Südwestdeutscher Verlag für Hochschulschriften, 2011.

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Londei, Paola, Anna La Teana, and Sébastien Ferreira-Cerca, eds. Archaeal Ribosomes: Biogenesis, Structure and Function. Frontiers Media SA, 2022. http://dx.doi.org/10.3389/978-2-88974-141-0.

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Hadjiolov, A. A. The Nucleolus and Ribosome Biogenesis (Cell Biology Monographs). Springer, 1985.

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Book chapters on the topic "Ribosome biogensis"

1

Oborská-Oplová, Michaela, Ute Fischer, Martin Altvater, and Vikram Govind Panse. "Eukaryotic Ribosome assembly and Nucleocytoplasmic Transport." In Ribosome Biogenesis, 99–126. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_7.

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AbstractThe process of eukaryotic ribosome assembly stretches across the nucleolus, the nucleoplasm and the cytoplasm, and therefore relies on efficient nucleocytoplasmic transport. In yeast, the import machinery delivers ~140,000 ribosomal proteins every minute to the nucleus for ribosome assembly. At the same time, the export machinery facilitates translocation of ~2000 pre-ribosomal particles every minute through ~200 nuclear pore complexes (NPC) into the cytoplasm. Eukaryotic ribosome assembly also requires >200 conserved assembly factors, which transiently associate with pre-ribosomal particles. Their site(s) of action on maturing pre-ribosomes are beginning to be elucidated. In this chapter, we outline protocols that enable rapid biochemical isolation of pre-ribosomal particles for single particle cryo-electron microscopy (cryo-EM) and in vitro reconstitution of nuclear transport processes. We discuss cell-biological and genetic approaches to investigate how the ribosome assembly and the nucleocytoplasmic transport machineries collaborate to produce functional ribosomes.
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Blanchet, Sandra, and Namit Ranjan. "Translation Phases in Eukaryotes." In Ribosome Biogenesis, 217–28. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_13.

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AbstractProtein synthesis in eukaryotes is carried out by 80S ribosomes with the help of many specific translation factors. Translation comprises four major steps: initiation, elongation, termination, and ribosome recycling. In this review, we provide a comprehensive list of translation factors required for protein synthesis in yeast and higher eukaryotes and summarize the mechanisms of each individual phase of eukaryotic translation.
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Jüttner, Michael, and Sébastien Ferreira-Cerca. "A Comparative Perspective on Ribosome Biogenesis: Unity and Diversity Across the Tree of Life." In Ribosome Biogenesis, 3–22. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_1.

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AbstractRibosomes are universally conserved ribonucleoprotein complexes involved in the decoding of the genetic information contained in messenger RNAs into proteins. Accordingly, ribosome biogenesis is a fundamental cellular process required for functional ribosome homeostasis and to preserve satisfactory gene expression capability.Although the ribosome is universally conserved, its biogenesis shows an intriguing degree of variability across the tree of life. These differences also raise yet unresolved questions. Among them are (a) what are, if existing, the remaining ancestral common principles of ribosome biogenesis; (b) what are the molecular impacts of the evolution history and how did they contribute to (re)shape the ribosome biogenesis pathway across the tree of life; (c) what is the extent of functional divergence and/or convergence (functional mimicry), and in the latter case (if existing) what is the molecular basis; (d) considering the universal ribosome conservation, what is the capability of functional plasticity and cellular adaptation of the ribosome biogenesis pathway?In this review, we provide a brief overview of ribosome biogenesis across the tree of life and try to illustrate some potential and/or emerging answers to these unresolved questions.
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Braun, Christina, Robert Knüppel, Jorge Perez-Fernandez, and Sébastien Ferreira-Cerca. "Non-radioactive In Vivo Labeling of RNA with 4-Thiouracil." In Ribosome Biogenesis, 199–213. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_12.

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AbstractRNA molecules and their expression dynamics play essential roles in the establishment of complex cellular phenotypes and/or in the rapid cellular adaption to environmental changes. Accordingly, analyzing RNA expression remains an important step to understand the molecular basis controlling the formation of cellular phenotypes, cellular homeostasis or disease progression. Steady-state RNA levels in the cells are controlled by the sum of highly dynamic molecular processes contributing to RNA expression and can be classified in transcription, maturation and degradation. The main goal of analyzing RNA dynamics is to disentangle the individual contribution of these molecular processes to the life cycle of a given RNA under different physiological conditions. In the recent years, the use of nonradioactive nucleotide/nucleoside analogs and improved chemistry, in combination with time-dependent and high-throughput analysis, have greatly expanded our understanding of RNA metabolism across various cell types, organisms, and growth conditions.In this chapter, we describe a step-by-step protocol allowing pulse labeling of RNA with the nonradioactive nucleotide analog, 4-thiouracil, in the eukaryotic model organism Saccharomyces cerevisiae and the model archaeon Haloferax volcanii.
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Pinz, Sophia, Eva Doskocil, and Wolfgang Seufert. "Thermofluor-Based Analysis of Protein Integrity and Ligand Interactions." In Ribosome Biogenesis, 247–57. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_15.

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AbstractThermofluor is a fluorescence-based thermal shift assay, which measures temperature-induced protein unfolding and thereby yields valuable information about the integrity of a purified recombinant protein. Analysis of ligand binding to a protein is another popular application of this assay. Thermofluor requires neither protein labeling nor highly specialized equipment, and can be performed in a regular real-time PCR instrument. Thus, for a typical molecular biology laboratory, Thermofluor is a convenient method for the routine assessment of protein quality. Here, we provide Thermofluor protocols using the example of Cdc123. This ATP-grasp protein is an essential assembly chaperone of the eukaryotic translation initiation factor eIF2. We also report on a destabilized mutant protein version and on the ATP-mediated thermal stabilization of wild-type Cdc123 illustrating protein integrity assessment and ligand binding analysis as two major applications of the Thermofluor assay.
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Sharma, Sunny, and Karl-Dieter Entian. "Chemical Modifications of Ribosomal RNA." In Ribosome Biogenesis, 149–66. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_9.

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AbstractCellular RNAs in all three kingdoms of life are modified with diverse chemical modifications. These chemical modifications expand the topological repertoire of RNAs, and fine-tune their functions. Ribosomal RNA in yeast contains more than 100 chemically modified residues in the functionally crucial and evolutionary conserved regions. The chemical modifications in the rRNA are of three types—methylation of the ribose sugars at the C2-positionAbstract (Nm), isomerization of uridines to pseudouridines (Ψ), and base modifications such as (methylation (mN), acetylation (acN), and aminocarboxypropylation (acpN)). The modifications profile of the yeast rRNA has been recently completed, providing an excellent platform to analyze the function of these modifications in RNA metabolism and in cellular physiology. Remarkably, majority of the rRNA modifications and the enzymatic machineries discovered in yeast are highly conserved in eukaryotes including humans. Mutations in factors involved in rRNA modification are linked to several rare severe human diseases (e.g., X-linked Dyskeratosis congenita, the Bowen–Conradi syndrome and the William–Beuren disease). In this chapter, we summarize all rRNA modifications and the corresponding enzymatic machineries of the budding yeast.
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Kern, Michael, and Sébastien Ferreira-Cerca. "Differential Translation Activity Analysis Using Bioorthogonal Noncanonical Amino Acid Tagging (BONCAT) in Archaea." In Ribosome Biogenesis, 229–46. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_14.

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AbstractThe study of protein production and degradation in a quantitative and time-dependent manner is a major challenge to better understand cellular physiological response. Among available technologies bioorthogonal noncanonical amino acid tagging (BONCAT) is an efficient approach allowing for time-dependent labeling of proteins through the incorporation of chemically reactive noncanonical amino acids like l-azidohomoalanine (L-AHA). The azide-containing amino-acid derivative enables a highly efficient and specific reaction termed click chemistry, whereby the azide group of the L-AHA reacts with a reactive alkyne derivate, like dibenzocyclooctyne (DBCO) derivatives, using strain-promoted alkyne–azide cycloaddition (SPAAC). Moreover, available DBCO containing reagents are versatile and can be coupled to fluorophore (e.g., Cy7) or affinity tag (e.g., biotin) derivatives, for easy visualization and affinity purification, respectively.Here, we describe a step-by-step BONCAT protocol optimized for the model archaeon Haloferax volcanii, but which is also suitable to harness other biological systems. Finally, we also describe examples of downstream visualization, affinity purification of L-AHA-labeled proteins and differential expression analysis.In conclusion, the following BONCAT protocol expands the available toolkit to explore proteostasis using time-resolved semiquantitative proteomic analysis in archaea.
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Merkl, Philipp E., Christopher Schächner, Michael Pilsl, Katrin Schwank, Catharina Schmid, Gernot Längst, Philipp Milkereit, Joachim Griesenbeck, and Herbert Tschochner. "Specialization of RNA Polymerase I in Comparison to Other Nuclear RNA Polymerases of Saccharomyces cerevisiae." In Ribosome Biogenesis, 63–70. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_4.

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AbstractIn archaea and bacteria the major classes of RNAs are synthesized by one DNA-dependent RNA polymerase (RNAP). In contrast, most eukaryotes have three highly specialized RNAPs to transcribe the nuclear genome. RNAP I synthesizes almost exclusively ribosomal (r)RNA, RNAP II synthesizes mRNA as well as many noncoding RNAs involved in RNA processing or RNA silencing pathways and RNAP III synthesizes mainly tRNA and 5S rRNA. This review discusses functional differences of the three nuclear core RNAPs in the yeast S. cerevisiae with a particular focus on RNAP I transcription of nucleolar ribosomal (r)DNA chromatin.
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Blanchet, Sandra, and Namit Ranjan. "In Vitro Assembly of a Fully Reconstituted Yeast Translation System for Studies of Initiation and Elongation Phases of Protein Synthesis." In Ribosome Biogenesis, 259–80. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_16.

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AbstractProtein synthesis is an essential and highly regulated cellular process. To facilitate the understanding of eukaryotic translation, we have assembled an in vitro translation system from yeast using purified components to recapitulate the initiation and elongation phases of protein synthesis. Here, we describe methods to express and purify the components of the translation system and the assays for their functional characterization.
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Yang, Jun, Peter Watzinger, and Sunny Sharma. "Mapping of the Chemical Modifications of rRNAs." In Ribosome Biogenesis, 181–97. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_11.

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AbstractCellular RNAs, both coding and noncoding, contain several chemical modifications. Both ribose sugars and nitrogenous bases are targeted for these chemical additions. These modifications are believed to expand the topological potential of RNA molecules by bringing chemical diversity to otherwise limited repertoire. Here, using ribosomal RNA of yeast as an example, a detailed protocol for systematically mapping various chemical modifications to a single nucleotide resolution by a combination of Mung bean nuclease protection assay and RP-HPLC is provided. Molar levels are also calculated for each modification using their UV (254 nm) molar response factors that can be used for determining the amount of modifications at different residues in other RNA molecules. The chemical nature, their precise location and quantification of modifications will facilitate understanding the precise role of these chemical modifications in cellular physiology.
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Conference papers on the topic "Ribosome biogensis"

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Menoyo, Sandra, Antonio Gentilella, and George Thomas. "Abstract B05: Characterization of the pre-ribosomal complex, which mediates the p53 Impaired Ribosome Biogenesis Checkpoint (IRBC)." In Abstracts: AACR Special Conference on Translational Control of Cancer: A New Frontier in Cancer Biology and Therapy; October 27-30, 2016; San Francisco, CA. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.transcontrol16-b05.

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Lessard, Frédéric, Véronique Bourdeau, Xavier Deschênes-Simard, Sebastian Igelmann, Marinieve Montero, and Gerardo Ferbeyre. "Abstract 2246: Senescence as a result of impaired ribosome biogenesis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2246.

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Dong, Zhixiong, Changjun Zhu, and Wei Jiang. "Abstract 835: hRrp15, a ribosome RNA processing protein, has profound function on nucleoli construction, ribosome biogenesis and cell proliferation." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-835.

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Shakirov, Yevgeniy. "Ribosome biogenesis pathway underlies establishment of telomere length set point in Arabidopsis." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1375852.

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Pearson, Richard B., Jennifer R. Devlin, Katherine M. Hannan, Nadine Hein, Megan J. Bywater, Gretchen Poortinga, Donald Cameron, et al. "Abstract 2735: Multi-point targeting of the synthetic lethal interactions between Myc, ribosome biogenesis and ribosome function cooperates to treat B-cell lymphoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2735.

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Sun, Xiao-Xin, and Mushui Dai. "Abstract 1104: Perturbation of 60S ribosomal biogenesis results in ribosomal protein L5 and L11-dependent p53 activation." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1104.

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Sheppard, Karen E., Natalie Brajanovski, Katherine M. Hannan, Jessica Ahearn, Jason Ellul, Denis Drygin, Sean O'Brien, Grant McArthur, Ross D. Hannan, and Richard B. Pearson. "Abstract 2718: Targeting ribosome biogenesis with CX5461 as a potential treatment for melanoma and ovarian cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2718.

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Penzo, Marianna, Lucia Casoli, Laura Sicuro, Alice Galibiati, Daniela Pollutri, Marzia Govoni, Claudio Ceccarelli, et al. "Abstract 5145: KDM2B expression regulates ribosome biogenesis and cancer cell growth in a p53-dependent manner." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-5145.

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Lessard, Frédéric, Véronique Bourdeau, Sebastian Igelmann, Xavier Deschênes-Simard, Marinieve Montero, and Gerardo Ferbeyre. "Abstract 1270: Ribosome biogenesis is reduced by oncogenic stress in normal cells and is sufficient to trigger cellular senescence." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1270.

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Devlin, Jennifer R., Richard J. Rebello, Katherine M. Hannan, Carleen Cullinane, Denis Drygin, Gail P. Risbridger, Luc Furic, Ross D. Hannan, and Richard B. Pearson. "Abstract 4809: Combination therapy targeting ribosome biogenesis and mRNA translation provides a novel and potent therapeutic approach to treat MYC-driven malignancy." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4809.

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