Academic literature on the topic 'Eukaryotic; Binding proteins; Gene expression'

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Journal articles on the topic "Eukaryotic; Binding proteins; Gene expression"

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Martín, Victoria, Miguel A. Rodríguez-Gabriel, W. Hayes McDonald, Stephen Watt, John R. Yates, Jürg Bähler, and Paul Russell. "Cip1 and Cip2 Are Novel RNA-Recognition-Motif Proteins That Counteract Csx1 Function during Oxidative Stress." Molecular Biology of the Cell 17, no. 3 (March 2006): 1176–83. http://dx.doi.org/10.1091/mbc.e05-09-0847.

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Eukaryotic cells reprogram their global patterns of gene expression in response to stress. Recent studies in Schizosaccharomyces pombe showed that the RNA-binding protein Csx1 plays a central role in controlling gene expression during oxidative stress. It does so by stabilizing atf1+ mRNA, which encodes a subunit of a bZIP transcription factor required for gene expression during oxidative stress. Here, we describe two related proteins, Cip1 and Cip2, that were identified by multidimensional protein identification technology (MudPIT) as proteins that coprecipitate with Csx1. Cip1 and Cip2 are cytoplasmic proteins that have RNA recognition motifs (RRMs). Neither protein is essential for viability, but a cip1Δ cip2Δ strain grows poorly and has altered cellular morphology. Genetic epistasis studies and whole genome expression profiling show that Cip1 and Cip2 exert posttranscriptional control of gene expression in a manner that is counteracted by Csx1. Notably, the sensitivity of csx1Δ cells to oxidative stress and their inability to induce expression of Atf1-dependent genes are partially rescued by cip1Δ and cip2Δ mutations. This study emphasizes the importance of a modulated mRNA stability in the eukaryotic stress response pathways and adds new information to the role of RNA-binding proteins in the oxidative stress response.
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Yao, Yunping, Changsheng Ouyang, Lu Jiang, Xiaoguang Liu, Qing Hao, Guozhong Zhao, and Bin Zeng. "Specificity of acyl-CoA binding protein to acyl-CoAs: influence on the lipid metabolism in Aspergillus oryzae." RSC Advances 6, no. 97 (2016): 94859–65. http://dx.doi.org/10.1039/c6ra20532a.

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Acyl-CoA binding protein (ACBP) is involved in lipid metabolism and regulation of gene expression in eukaryotic cells, however, the specific functional roles of this important class of proteins remain to be elucidated.
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de Koning, Bart, Fabian Blombach, Hao Wu, Stan J. J. Brouns, and John van der Oost. "Role of multiprotein bridging factor 1 in archaea: bridging the domains?" Biochemical Society Transactions 37, no. 1 (January 20, 2009): 52–57. http://dx.doi.org/10.1042/bst0370052.

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MBF1 (multiprotein bridging factor 1) is a highly conserved protein in archaea and eukaryotes. It was originally identified as a mediator of the eukaryotic transcription regulator BmFTZ-F1 (Bombyx mori regulator of fushi tarazu). MBF1 was demonstrated to enhance transcription by forming a bridge between distinct regulatory DNA-binding proteins and the TATA-box-binding protein. MBF1 consists of two parts: a C-terminal part that contains a highly conserved helix–turn–helix, and an N-terminal part that shows a clear divergence: in eukaryotes, it is a weakly conserved flexible domain, whereas, in archaea, it is a conserved zinc-ribbon domain. Although its function in archaea remains elusive, its function as a transcriptional co-activator has been deduced from thorough studies of several eukaryotic proteins, often indicating a role in stress response. In addition, MBF1 was found to influence translation fidelity in yeast. Genome context analysis of mbf1 in archaea revealed conserved clustering in the crenarchaeal branch together with genes generally involved in gene expression. It points to a role of MBF1 in transcription and/or translation. Experimental data are required to allow comparison of the archaeal MBF1 with its eukaryotic counterpart.
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Patrick, Ryan M., Jessica C. H. Lee, Jade R. J. Teetsel, Soo-Hyun Yang, Grace S. Choy, and Karen S. Browning. "Discovery and characterization of conserved binding of eIF4E 1 (CBE1), a eukaryotic translation initiation factor 4E–binding plant protein." Journal of Biological Chemistry 293, no. 44 (September 13, 2018): 17240–47. http://dx.doi.org/10.1074/jbc.ra118.003945.

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In many eukaryotes, translation initiation is regulated by proteins that bind to the mRNA cap–binding protein eukaryotic translation initiation factor 4E (eIF4E). These proteins commonly prevent association of eIF4E with eIF4G or form repressive messenger ribonucleoproteins that exclude the translation machinery. Such gene-regulatory mechanisms in plants, and even the presence of eIF4E-interacting proteins other than eIF4G (and the plant-specific isoform eIFiso4G, which binds eIFiso4E), are unknown. Here, we report the discovery of a plant-specific protein, conserved binding of eIF4E 1 (CBE1). We found that CBE1 has an evolutionarily conserved eIF4E-binding motif in its N-terminal domain and binds eIF4E or eIFiso4E in vitro. CBE1 thereby forms cap-binding complexes and is an eIF4E-dependent constituent of these complexes in vivo. Of note, plant mutants lacking CBE1 exhibited dysregulation of cell cycle–related transcripts and accumulated higher levels of mRNAs encoding proteins involved in mitosis than did WT plants. Our findings indicate that CBE1 is a plant protein that can form mRNA cap–binding complexes having the potential for regulating gene expression. Because mammalian translation factors are known regulators of cell cycle progression, we propose that CBE1 may represent such first translation factor–associated plant-specific cell cycle regulator.
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Xu, Ming-yan, Ju-li Liu, Ren-li Zhang, and Yu-cai Fu. "Isolation of a novel ras gene from Trichomonas vaginalis: a possible evolutionary ancestor of the Ras and Rap genes of higher eukaryotesThis paper is one of a selection of papers in this Special Issue, entitled International Symposium on Recent Advances in Molecular, Clinical, and Social Medicine, and has undergone the Journal's usual peer-review process." Biochemistry and Cell Biology 85, no. 2 (April 2007): 239–45. http://dx.doi.org/10.1139/o07-008.

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The Ras subfamily proteins are small, monomeric GTP-binding proteins with vital roles in regulating eukaryotic signal transduction pathways. Gene duplication and divergence have been postulated as the mechanism by which such family members have evolved their specific functions. A cDNA clone of TvRsp was isolated and sequenced from a cDNA expression library of the primitive eukaryote Trichomonas vaginalis . The genomic DNA corresponding to the cDNA sequence was amplified by PCR and sequenced. Sequence analysis suggested that TvRsp was an intronless gene. This gene encoded a protein of 181 amino acids and contained the 5 conserved G domains that designated it as a Ras or Rap subfamily member. However, the deduced amino acid sequence shared only 34%–37% overall identity with other Ras subfamily members of different species, and the presence of motifs characteristic of both the Ras and Rap families of GTPase confused the familial classification of this gene. Phylogenetic analysis showed its origins at the divergence point of the Ras/Rap families and suggested that TvRsp was a possible evolutionary ancestral gene of the ras/rap genes of higher eukaryotes. This information was of importance not only from the perspective of understanding the evolution and diversity of eukaryotic signal transduction pathways but also in providing a framework by which to understand protein processing in the growth and differentiation of single-celled microorganisms.
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Harvey, Robert, Veronica Dezi, Mariavittoria Pizzinga, and Anne E. Willis. "Post-transcriptional control of gene expression following stress: the role of RNA-binding proteins." Biochemical Society Transactions 45, no. 4 (July 14, 2017): 1007–14. http://dx.doi.org/10.1042/bst20160364.

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The ability of mammalian cells to modulate global protein synthesis in response to cellular stress is essential for cell survival. While control of protein synthesis is mediated by the regulation of eukaryotic initiation and elongation factors, RNA-binding proteins (RBPs) provide a crucial additional layer to post-transcriptional regulation. RBPs bind specific RNA through conserved RNA-binding domains and ensure that the information contained within the genome and transcribed in the form of RNA is exported to the cytoplasm, chemically modified, and translated prior to folding into a functional protein. Thus, this group of proteins, through mediating translational reprogramming, spatial reorganisation, and chemical modification of RNA molecules, have a major influence on the robust cellular response to external stress and toxic injury.
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Das, Aparajita, and Vijayakumar Boggaram. "Proteasome dysfunction inhibits surfactant protein gene expression in lung epithelial cells: mechanism of inhibition of SP-B gene expression." American Journal of Physiology-Lung Cellular and Molecular Physiology 292, no. 1 (January 2007): L74—L84. http://dx.doi.org/10.1152/ajplung.00103.2006.

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Surfactant proteins maintain lung function through their actions to reduce alveolar surface tension and control of innate immune responses in the lung. The ubiquitin proteasome pathway is responsible for the degradation of majority of intracellular proteins in eukaryotic cells, and proteasome dysfunction has been linked to the development of neurodegenerative, cardiac, and other diseases. Proteasome function is impaired in interstitial lung diseases associated with surfactant protein C (SP-C) mutation mapping to the BRICHOS domain located in the proSP-C protein. In this study we determined the effects of proteasome inhibition on surfactant protein expression in H441 and MLE-12 lung epithelial cells to understand the relationship between proteasome dysfunction and surfactant protein gene expression. Proteasome inhibitors lactacystin and MG132 reduced the levels of SP-A, SP-B, and SP-C mRNAs in a concentration-dependent manner in H441 and MLE-12 cells. In H441 cells, lactacystin and MG132 inhibition of SP-B mRNA was associated with similar decreases in SP-B protein, and the inhibition was due to inhibition of gene transcription. Proteasome inhibitors decreased thyroid transcription factor-1 (TTF-1)/Nkx2.1 DNA binding activity, and the reduced TTF-1 DNA binding activity was due to reduced expression levels of TTF-1 protein. These data indicated that the ubiquitin proteasome pathway is essential for the maintenance of surfactant protein gene expression and that disruption of this pathway inhibits surfactant protein gene expression via reduced expression of TTF-1 protein.
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Corry, Gareth N., and D. Alan Underhill. "Subnuclear compartmentalization of sequence-specific transcription factors and regulation of eukaryotic gene expression." Biochemistry and Cell Biology 83, no. 4 (August 1, 2005): 535–47. http://dx.doi.org/10.1139/o05-062.

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To date, the majority of the research regarding eukaryotic transcription factors has focused on characterizing their function primarily through in vitro methods. These studies have revealed that transcription factors are essentially modular structures, containing separate regions that participate in such activities as DNA binding, protein–protein interaction, and transcriptional activation or repression. To fully comprehend the behavior of a given transcription factor, however, these domains must be analyzed in the context of the entire protein, and in certain cases the context of a multiprotein complex. Furthermore, it must be appreciated that transcription factors function in the nucleus, where they must contend with a variety of factors, including the nuclear architecture, chromatin domains, chromosome territories, and cell-cycle-associated processes. Recent examinations of transcription factors in the nucleus have clarified the behavior of these proteins in vivo and have increased our understanding of how gene expression is regulated in eukaryotes. Here, we review the current knowledge regarding sequence-specific transcription factor compartmentalization within the nucleus and discuss its impact on the regulation of such processes as activation or repression of gene expression and interaction with coregulatory factors.Key words: transcription, subnuclear localization, chromatin, gene expression, nuclear architecture.
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Pacheco, Almudena, and Encarnacion Martinez-Salas. "Insights into the Biology of IRES Elements through Riboproteomic Approaches." Journal of Biomedicine and Biotechnology 2010 (2010): 1–12. http://dx.doi.org/10.1155/2010/458927.

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Translation initiation is a highly regulated process that exerts a strong influence on the posttranscriptional control of gene expression. Two alternative mechanisms govern translation initiation in eukaryotic mRNAs, the cap-dependent initiation mechanism operating in most mRNAs, and the internal ribosome entry site (IRES)-dependent mechanism, first discovered in picornaviruses. IRES elements are highly structured RNA sequences that, in most instances, require specific proteins for recruitment of the translation machinery. Some of these proteins are eukaryotic initiation factors. In addition, RNA-binding proteins (RBPs) play a key role in internal initiation control. RBPs are pivotal regulators of gene expression in response to numerous stresses, including virus infection. This review discusses recent advances on riboproteomic approaches to identify IRES transacting factors (ITAFs) and the relationship between RNA-protein interaction and IRES activity, highlighting the most relevant features on picornavirus and hepatitis C virus IRESs.
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Kamenska, Anastasiia, Clare Simpson, and Nancy Standart. "eIF4E-binding proteins: new factors, new locations, new roles." Biochemical Society Transactions 42, no. 4 (August 1, 2014): 1238–45. http://dx.doi.org/10.1042/bst20140063.

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The cap-binding translation initiation factor eIF4E (eukaryotic initiation factor 4E) is central to protein synthesis in eukaryotes. As an integral component of eIF4F, a complex also containing the large bridging factor eIF4G and eIF4A RNA helicase, eIF4E enables the recruitment of the small ribosomal subunit to the 5′ end of mRNAs. The interaction between eIF4E and eIF4G via a YXXXXLϕ motif is regulated by small eIF4E-binding proteins, 4E-BPs, which use the same sequence to competitively bind eIF4E thereby inhibiting cap-dependent translation. Additional eIF4E-binding proteins have been identified in the last 10–15 years, characterized by the YXXXXLϕ motif, and by interactions (many of which remain to be detailed) with RNA-binding proteins, or other factors in complexes that recognize the specific mRNAs. In the present article, we focus on the metazoan 4E-T (4E-transporter)/Cup family of eIF4E-binding proteins, and also discuss very recent examples in yeast, fruitflies and humans, some of which predictably inhibit translation, while others may result in mRNA decay or even enhance translation; altogether considerably expanding our understanding of the roles of eIF4E-binding proteins in gene expression regulation.
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Dissertations / Theses on the topic "Eukaryotic; Binding proteins; Gene expression"

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Crowther, Daniel. "Cloning and characterization of Cpf1P from Schizosaccharomyces pombe." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.320634.

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Kiesler, Eva. "Isolation and functional characterization of Hrp65-binding proteins in Chironomus tentans." Doctoral thesis, Stockholm : Institutionen för molekylärbiologi och funktionsgenomik, Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-218.

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Tang, Terry, and University of Lethbridge Faculty of Arts and Science. "Mathematical modeling of eukaryotic gene expression." Thesis, Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, 2010, 2010. http://hdl.handle.net/10133/2567.

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Using the Gillespie algorithm, the export of the mRNA molecules from their transcription site to the nuclear pore complex is simulated. The effect of various structures in the nu- cleus on the efficiency of export is discussed. The results show that having some of the space filled by chromatin near the mRNA synthesis site shortens the transport time. Next, the complete eukaryotic gene expression including transcription, splicing, mRNA export, translation, and mRNA degradation is modeled using delay stochastic simulation. This allows for the study of stochastic effects during the process and on the protein production rate patterns. Various protein production patterns can be produced by adjusting the poly-A tail length of the mRNA and the promoter efficiency of the gene. After that, the opposing effects of the chromatin density on the seeking time of the transcription factors for the promoter and the exit time of the mRNA product are discussed.
xi, 102 leaves ; 28 cm
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Lahudkar, Shweta L. "REGULATION OF EUKARYOTIC GENE EXPRESSION BY mRNA CAP BINDING COMPLEX AND CAPPING MACHINERY." OpenSIUC, 2014. https://opensiuc.lib.siu.edu/dissertations/834.

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A characteristic feature of gene expression in eukaryotes is the addition of a 5' terminal 7-methylguanine "cap" to nascent pre-messenger RNA (mRNA) in the nucleus. It is the 5'capping process, which proves vital to creating a mature mRNA. The synthesis of an mRNA followed by its capping is a complex undertaking which requires a set of protein factors. The capped mRNA is then exclusively bound by a cap-binding complex (CBC). CBC shields mRNA from exonucleases as well as regulates downstream post-transcriptional events, translational initiation and nonsense mediated mRNA decay (NMD). Any misregulation during capping or in the binding of CBC can lead a number of diseases/disorders. Thus, the process and regulation of capping and CBC binding to mRNA are important fields to study the control of gene expression. Over the years, capping apparatus and CBC have been implicated in post-transcriptional regulation. However, it is not yet known whether CBC plays any role in controlling transcriptional initiation or elongation. Thus, the major research focus in my thesis had been to analyze the role of CBC and capping enzymes in regulation of transcriptional initiation and elongation. The results have revealed the role of CBC in stimulating the formation of pre-initiation complex (PIC) at the promoter in vivo via Mot1p (modifier of transcription). Subsequently, we have demonstrated the roles of CBC in transcription elongation, splicing and nuclear export of mRNA. Interestingly, we find that the capping enzyme, Cet1p, decreases promoter proximal accumulation of RNA polymerase II. These results support that Cet1p promotes the release of paused-RNA polymerase II to get engaged into elongating form for productive transcription. Such function of Cet1p appears to be mediated via the Facilitates chromatin transcription (FACT) complex. We find that FACT is targeted to the active gene by the N-terminal domain of Cet1p independently of its capping activity. In the absence of Cet1p, recruitment of FACT to the active gene is impaired, leading to paused-RNA polymerase II. Collectively, the results of my thesis work provide significant insight on the regulation of gene expression by CBC and capping enzyme, Cet1p.
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Waters, Lorna Catherine. "Solution structures of proteins and complexes involved in the regulation of eukaryotic gene expression." Thesis, University of Leicester, 2007. http://hdl.handle.net/2381/29722.

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The initial work focused on the interaction between the general coactivator CBP (SID domain) and members of the p160 family of coactivators (AD1 domain), which is a key step in the activation of transcription by nuclear receptors. The solution structure of the CBP SID / SRC1 AD1 complex described in this thesis shows that the two helical domains are intimately associated, with the first helix in SRC1 AD1 and the first three helices in CBP SID forming a four helix bundle, which is capped by the fourth helix of the AD 1 domain. Comparisons with the structure of the related CBP SID / ACTR AD 1 complex showed that while the CBP SID domain adopts a similar fold in complex with different p160 proteins, the topologies of the AD1 domains are strikingly different, a feature that is likely to contribute to functional specificity of these complexes. The second part of the work described here focused on the interaction between the MA-3 domains of the tumour suppressor Pdcd4 and the translation factor eIF4A, which has been shown to inhibit cap-dependent translation. The C-terminal MA-3 domain (Pdcd4 MA-3C) was shown to consist of three atypical HEAT repeats capped by a final helix. This domain was found to interact with the N-terminal domain of eIF4A through a conserved surface region. The comparison of NMR spectra obtained from Pdcd4 MA-3 C and the tandem MA-3 region strongly suggests that the tandem MA-3 region is composed of two equivalent domains connected by a semi-flexible linker. The high resolution structural information obtained provides important insights into the interactions and functional specificity of the protein complexes studied.
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Mehraein-Ghomi, Farideh. "Analysis of the assembly of a eukaryotic glucose transporter into the Escherichia coli cytoplasmic membrane." Thesis, University of Sussex, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284076.

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Kiełbasa, Szymon M. "Bioinformatics of eukaryotic gene regulation." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2006. http://dx.doi.org/10.18452/15562.

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Die Aufklärung der Mechanismen zur Kontrolle der Genexpression ist eines der wichtigsten Probleme der modernen Molekularbiologie. Detaillierte experimentelle Untersuchungen sind enorm aufwändig aufgrund der komplexen und kombinatorischen Wechselbeziehungen der beteiligten Moleküle. Infolgedessen sind bioinformatische Methoden unverzichtbar. Diese Dissertation stellt drei Methoden vor, die die Vorhersage der regulatorischen Elementen der Gentranskription verbessern. Der erste Ansatz findet Bindungsstellen, die von den Transkriptionsfaktoren erkannt werden. Dieser sucht statistisch überrepräsentierte kurze Motive in einer Menge von Promotersequenzen und wird erfolgreich auf das Genom der Bäckerhefe angewandt. Die Analyse der Genregulation in höheren Eukaryoten benötigt jedoch fortgeschrittenere Techniken. In verschiedenen Datenbanken liegen Hunderte von Profilen vor, die von den Transkriptionsfaktoren erkannt werden. Die Ähnlichkeit zwischen ihnen resultiert in mehrfachen Vorhersagen einer einzigen Bindestelle, was im nachhinein korrigiert werden muss. Es wird eine Methode vorgestellt, die eine Möglichkeit zur Reduktion der Anzahl von Profilen bietet, indem sie die Ähnlichkeiten zwischen ihnen identifiziert. Die komplexe Natur der Wechselbeziehung zwischen den Transkriptionsfaktoren macht jedoch die Vorhersage von Bindestellen schwierig. Auch mit einer Verringerung der zu suchenden Profile sind die Resultate der Vorhersagen noch immer stark fehlerbehafted. Die Zuhilfenahme der unabhängigen Informationsressourcen reduziert die Häufigkeit der Falschprognosen. Die dritte beschriebene Methode schlägt einen neuen Ansatz vor, die die Gen-Anotation mit der Regulierung von multiplen Transkriptionsfaktoren und den von ihnen erkannten Bindestellen assoziiert. Der Nutzen dieser Methode wird anhand von verschiedenen wohlbekannten Sätzen von Transkriptionsfaktoren demonstriert.
Understanding the mechanisms which control gene expression is one of the fundamental problems of molecular biology. Detailed experimental studies of regulation are laborious due to the complex and combinatorial nature of interactions among involved molecules. Therefore, computational techniques are used to suggest candidate mechanisms for further investigation. This thesis presents three methods improving the predictions of regulation of gene transcription. The first approach finds binding sites recognized by a transcription factor based on statistical over-representation of short motifs in a set of promoter sequences. A succesful application of this method to several gene families of yeast is shown. More advanced techniques are needed for the analysis of gene regulation in higher eukaryotes. Hundreds of profiles recognized by transcription factors are provided by libraries. Dependencies between them result in multiple predictions of the same binding sites which need later to be filtered out. The second method presented here offers a way to reduce the number of profiles by identifying similarities between them. Still, the complex nature of interaction between transcription factors makes reliable predictions of binding sites difficult. Exploiting independent sources of information reduces the false predictions rate. The third method proposes a novel approach associating gene annotations with regulation of multiple transcription factors and binding sites recognized by them. The utility of the method is demonstrated on several well-known sets of transcription factors. RNA interference provides a way of efficient down-regulation of gene expression. Difficulties in predicting efficient siRNA sequences motivated the development of a library containing siRNA sequences and related experimental details described in the literature. This library, presented in the last chapter, is publicly available at http://www.human-sirna-database.net
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Dörr, Katrin Zaragoza. "Molecular mechanisms of gene activation and gene expression mediated by CCAAT/enhancer binding proteins." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2008. http://dx.doi.org/10.18452/15873.

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Der Transkriptionsfaktor CCAAT/Enhancer-Binding Protein alpha (C/EBPa) koordiniert Proliferationshemmung und Differenzierung von myeloiden VorlŠuferzellen und Adipozyten. C/EBPa ist ein transkriptioneller Aktivator von abstammungspezifischen Genen und blockiert den Zellzyklus durch Repression von proliferationsfšrdernden E2F Zielgenen. Die hier gezeigten Daten zeigen, dass auch umgekehrt E2F die transkriptionelle und differenzierungsfšrdernde AktivitŠt von C/EBPa entgegenwirkt. Somit besitzen E2F-C/EBPa eine zentrale Schalterfunktion zwischen Proliferation und Differenzierung. Der Repressionsmechanismus durch E2F ist in mehreren Aspekten neuartig: Zum erstenmal wurde gezeigt, dass E2F einen anderen Transkriptionsfaktor reprimieren kann. E2F reprimiert die transkriptionelle AktivitŠt von C/EBPa ohne Bindung an cis-regulatorischen Elemente, sondern durch direkte Protein-Protein Interaktionen, die die Bindung von C/EBPa an DNA verhindern. Diese Form der transkriptionellen Repression geschieht unabhŠngig von "Pocket-Proteinen''". Patienten mit Akuter Myeloiden LeukŠmie (AML) weisen hŠufig eine gestšrte DNA Bindung von C/EBPa auf, welche ursachlich fŸr granulozitŠren Funktionsstšrungen sein kšnnte. Daher wŠre es wichtig zu analysieren ob E2F die DNA Bindung von C/EBPa in AML Patienten beeintrŠchtigt und ob auf E2F gerichtete Therapien granulozitŠre Reifung wiederherstellen. C/EBPa blockiert Zellproliferation durch vielseitigen Mechanismen. Hier wurde gezeigt, dass C/EBPa mit UBF1, dem Co-Aktivator der RNA Polymerase I, an chromosomalen Foci positioniert wird. Eine €hnlichkeit zu anderen fokalen Strukturen suggeriert, dass C/EBPa die Transkription von Polymerase I regulierten rRNA Gene reprimieren und somit ribosomale Biogenese beeintrŠchtigen kšnnte. Die Assoziation zwischen C/EBPa und UBF1 wird durch die Histon-Methyltransferase SUV39H1 stimuliert. Demnach kšnnte die antiproliferative Funktion von C/EBPa nicht nur auf der Regulierung von RNA Pol II-abhŠngiger Transkription, sondern auch auf der Repression von RNA Pol I regulierter rRNA Synthese basieren.
The transcription factor CCAAT/Enhancer-Binding Protein alpha (C/EBPa) coordinates proliferation arrest and differentiation of myeloid progenitors and adipocytes. C/EBPa acts as a transcriptional activator of lineage specific genes and blocks the cell cycle by repressing transcription of E2F-regulated genes. Data presented here suggest that also inversely E2F interferes with the transcriptional activity of C/EBPa, counteracting C/EBPa-mediated differentiation processes. Thus, E2F-C/EBPa are part of a switch mechanism between proliferation and differentiation. The mechanism by which E2F suppresses C/EBPa-mediated transactivation is novel in several aspects. E2F acts as a co-repressor of another transcription factor, C/EBPa, without binding to cis-regulatory elements, but by direct protein-protein interactions that abolish the binding of C/EBPa to DNA. This mechanism of transcriptional repression occurs independent of pocket proteins. Disturbed DNA binding of C/EBPa is often observed in AML patients suggesting a causative role in granulocytic disorders. Thus, it would be of main interest to analyze whether E2F mediates disruption of C/EBPa''s DNA-binding in AML patients and whether therapies directed against E2F could restore granulocytic maturation. Despite the extensive knowledge of mechanisms involved in the inhibitory function of C/EBPa, it has not been addressed whether C/EBPa may impinge on cell proliferation by affecting the ribosomal biogenesis of a cell. This work demonstrates an association of C/EBPa to the RNA Pol I transcription factor UBF1, both proteins retained in large chromosomal foci. Similarities to other focal structures associated to UBF1, suggest that C/EBPa may repress transcription of Pol I-transcribed rRNA genes, and thus affect ribosomal biogenesis. The enrichment of C/EBPa at sites of UBF1 is induced by the histone methyltransferase SUV39H1. Thus, C/EBPa may not only control lineage commitment and cell proliferation by regulating genes transcribed by RNA Pol II, but also may act as a repressor of RNA Pol I mediated rRNA synthesis.
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Kiri, Arpna. "The isolation and function of the 3'untranslated region of the myosin heavy chain genes of skeletal muscle." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325611.

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Walton, Cherie. "Incorporation of Listeriolysin O into a ligand-based carrier system resulting in enhancement of gene expression /." Click for abstract, 1998. http://library.ctstateu.edu/ccsu%5Ftheses/1509.html.

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Thesis (M.A.)--Central Connecticut State University, 1998.
Thesis advisor: Thomas King. "... in partial fulfillment of the requirements for the degree of Master of Arts in Biological Sciences." Includes bibliographical references (leaves 49-52).
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Books on the topic "Eukaryotic; Binding proteins; Gene expression"

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Yamaguchi, Masayoshi. Regucalcin: Genomics, cell regulation, and disease. Hauppauge, N.Y: Nova Science Publishers, 2011.

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C, Baxter R., Gluckman Peter D, and Rosenfeld Ron G, eds. The insulin-like growth factors and their regulatory proteins: Proceedings of the Third International Symposium on Insulin-Like Growth Factors, Sydney, 6-10 February 1994. Amsterdam: Excerpta Medica, 1994.

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Heat Shock Response of Eukaryotic Cells. Springer, 1985.

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E, Krebs Jocelyn, Goldstein Elliott S, Kilpatrick Stephen T, Lewin Benjamin, and Lewin Benjamin, eds. Lewin's essential genes. 2nd ed. Sudbury, Mass: Jones and Bartlett Publishers, 2009.

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Krebs, Jocelyn E., Elliott S. Goldstein, and Stephen T. Kilpatrick. Lewin's Essential GENES. Jones & Bartlett Learning, LLC, 2020.

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Benjamin, Lewin, Lewin Benjamin, and Lewin Benjamin, eds. Essential genes. 2nd ed. Sudbury, Mass: Jones and Bartlett Publishers, 2009.

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Global strategies for disease detection and treatment: Proteomics. Amsterdam: International Organisations Services, 2001.

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Hanash, S. Global Strategies for Disease Detection and Treatment (Disease Markers). Ios Pr Inc, 2002.

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Palzkill, Timothy. Proteomics. Kluwer Academic Publishers, 2002.

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Palzkill, Timothy. Proteomics. Springer, 2013.

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Book chapters on the topic "Eukaryotic; Binding proteins; Gene expression"

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Edery, Isaac, Jerry Pelletier, and Nahum Sonenberg. "Role of Eukaryotic Messenger RNA Cap-Binding Protein in Regulation of Translation." In Translational Regulation of Gene Expression, 335–66. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5365-2_15.

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Wasylyk, B. "Promoter Elements of Eukaryotic Protein-Coding Genes." In Chromosomal Proteins and Gene Expression, 103–19. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_7.

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Hofmann, Wilma A., and Primal de Lanerolle. "Actin, Actin-Related Proteins and Actin-Binding Proteins in Transcriptional Control." In Gene Expression and Regulation, 503–17. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-40049-5_31.

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Azorin, Fernando, and Alexander Rich. "Z-DNA and its Binding Proteins." In Chromosomal Proteins and Gene Expression, 189–201. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_13.

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Kadonaga, James T., Michael R. Briggs, and Robert Tjian. "Eukaryotic Transcriptional Specificity Conferred by DNA-Binding Proteins." In New Frontiers in the Study of Gene Functions, 87–98. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1845-3_7.

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Mazza, Davide, Sourav Ganguly, and James G. McNally. "Monitoring Dynamic Binding of Chromatin Proteins In Vivo by Single-Molecule Tracking." In Imaging Gene Expression, 117–37. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-526-2_9.

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van Bilsen, Marc, Ger J. van der Vusse, Andries J. Gilde, Martijn Lindhout, and Karin A. J. M. van der Lee. "Peroxisome proliferator-activated receptors: Lipid binding proteins controling gene expression." In Cellular Lipid Binding Proteins, 131–38. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4419-9270-3_17.

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Bar-Peled, Maor, Diane C. Bassham, and Natasha V. Raikhel. "Transport of proteins in eukaryotic cells: more questions ahead." In Post-Transcriptional Control of Gene Expression in Plants, 223–49. Dordrecht: Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-0353-1_10.

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Toulmé, Jean-Jacques. "Stacking Interactions: The Key Mechanism for Binding of Proteins to Single-Stranded Regions of Native and Damaged Nucleic Acids?" In Chromosomal Proteins and Gene Expression, 263–86. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_18.

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Hardy, Simon. "Export of Proteins from Bacteria and Translocation of Proteins Across the Endoplasmic Reticulum of Eukaryotic Cells; a Comparison." In Post-transcriptional Control of Gene Expression, 221–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60929-9_19.

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Conference papers on the topic "Eukaryotic; Binding proteins; Gene expression"

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Pannekok, H., A. J. Van Zonneveid, C. J. M. de vries, M. E. MacDonald, H. Veerman, and F. Blasi. "FUNCTIONAL PROPERTIES OF DELETION-MUTANTS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643724.

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Over the past twenty-five years, genetic methods have generated a wealth of information on the regulation and the structure-function relationship of bacterial genes.These methods are based on the introduction of random mutations in a gene to alter its function. Subsequently, genetic techniques cure applied to localize the mutation, while the nature of the impairedfunction could be determined using biochemical methods. Classic examples of this approach is now considered to be the elucidation of the structure and function of genes, constituting the Escherichia coli lactose (lac) and tryptophan (trp) operons,and the detailed establishment of the structure and function of the repressor (lacl) of the lac operon. Recombinant DNA techniques and the development of appropriate expression systems have provided the means both to study structure and functionof eukaryotic (glyco-) proteins and to create defined mutations with a predestinedposition. The rationale for the construction of mutant genes should preferentiallyrely on detailed knowledge of the three-dimensional structure of the gene product.Elegant examples are the application of in vitro mutagenesis techniques to substitute amino-acid residues near the catalytic centre of subtilisin, a serine proteasefrom Bacillus species and to substituteanamino acid in the reactive site (i.e. Pi residue; methionine) of α-antitrypsin, a serine protease inhibitor. Such substitutions have resulted into mutant proteins which are less susceptible to oxidation and, in some cases, into mutant proteins with a higher specific activity than the wild-type protein.If no data are available on the ternary structure of a protein, other strategies have to be developed to construct intelligent mutants to study the relation between the structure and the function of a eukaryotic protein. At least for a number of gene families, the gene structure is thought to be created by "exon shuffling", an evolutionary recombinational process to insert an exon or a set of exons which specify an additional structural and/or functional domain into a pre-existing gene. Both the structure of the tissue-type plasminogen activator protein(t-PA) and the t-PA gene suggest that this gene has evolved as a result of exon shuffling. As put forward by Gilbert (Science 228 (1985) 823), the "acid test"to prove the validity of the exon shuffling theory is either to delete, insert or to substitute exon(s) (i.e. in the corresponding cDNA) and toassay the properties of the mutant proteins to demonstrate that an exon or a set of adjacent exons encode (s) an autonomousfunction. Indeed, by the construction of specific deletions in full-length t-PA cDNA and expression of mutant proteins intissue-culture cells, we have shown by this approach that exon 2 of thet-PA gene encodes the function required forsecretion, exon 4 encodes the "finger" domain involved in fibrin binding(presumably on undegraded fibrin) and the set of exons 8 and 9 specifies kringle 2, containing a lysine-binding sit(LBS) which interacts with carboxy-terminal lysines, generated in fibrin after plasmic digestion. Exons 10 through 14 encode the carboxy-ter-minal light chain of t-PA and harbor the catalytic centre of the molecule and represents the predominant "target site" for the fast-acting endothelial plasminogen activator inhibitor (PAI-1).As a follow-up of this genetic approach to construct deletion mutants of t-PA, we also created substitution mutants of t-PA. Different mutants were constructed to substitute cDNA encoding thelight chain of t-PA by cDNA encoding the B-chain of urokinase (u-PA), in order to demonstrate that autonomous structural and functional domains of eitherone of the separate molecules are able toexert their intrinsic properties in a different context (C.J.M. de Vries et al., this volume). The possibilities and the limitations of this approach to study the structure and the function of t-PA and of other components of the fibrinolytic process will be outlined.
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Beck, George R., Roberta Carboni, Michael Van Scoy, Brad Zerler, and Elizabeth Moran. "GENE EXPRESSION IN pRB/p300-COMPROMISED MC3T3-E1 CELLS: OSTEOPONTIN." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.304.

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El-Tanani, Mohamed, Roger Barraclough, Mark C. Wilkinson, and Philip S. Rudland. "METASTASIS-INDUCING DNA REGULATES THE EXPRESSION OF THE OSTEOPONTIN GENE BY BINDING THE TRANSCRIPTION FACTOR TCF-4." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.238.

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Xie, Zhonglin, Mahipal Singh, and Krishna Singh. "REGULATION OF OSTEOPONTIN GENE EXPRESSION IN ADULT RAT CARDIAC FIBROBLASTS BY ANGIOTENSIN II AND INTERLEUKIN 1-[beta]: ROLE OF MAPKS SUPERFAMILY." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.280.

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Furis, B. C., M. J. Jorgensem, M. J. Rabiet, A. B. Contor, C. L. Brown, C. B. Shoemaker, and B. Furie. "RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.

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Factor IX and prothrombin vitamin K-dependent proteins that participate in blood coagulation undergo post-translationalmodification in which glutamic acid residues in the amino terminus of the protein are converted to gamma-carboxyglutamic acid residues. This modification confers divalent metal ion binding ability upon the proteins.As a consequence of binding divalent metal ions these proteins undergoconformational changes necessary for biological function.The vitamin K-dependent proteins are synthesized with an NH2-terminal extension. The region distal to the NH2-terminus of the mature protein is a prototypic signal sequence while the proximal region is a propeptide with homology among the vitamin K-dependent proteins. The boundary between the pre and pro sequences has been established for factor IX by analysis of three naturally occurring factor IX mutants factor IX Cambridge factor IX Oxford-3 and factor IX San Dimas, in which processing is incomplete.For human factor IX the propeptide extends from residue -18 to -1. The homology among the propeptides of vitamin K-dependent proteins suggests that the propeptide may designate adjacent gamma-carboxyglutamic acids for carboxylation. To test this hypothesis alterations in sequence were introduced into the propeptide region of human factor IX cDNA by oligonucleotide directed site specific mutagenesis.Mutated genes were expressed in Chinese hamster ovary cells. Rapid and efficient isolationof the mutant proteins by immunoaffinity chromatography permitted detailed analysis of the mutants on quantities of protein easily obtainable at low expression levels. The extent of gamma-carboxylation was assessed by the ability of the mutant proteins to interact with conformation specific antibodies directed against the gamma-carboxyglutamic acid-dependent metal stabilized native structure of factor IX as well as by direct amino acid analysis. Unmodified recombinant factor IX contained, on average, 9 gamma-carboxyglutamic acid residues, as compared to 12 for plasma factor IX. About 70% of the recombinant wild type factor IX bound to the conformation specific antibodies. Deletion of the propiece or point mutations at residues -10 or -16 led to secretion of uncarboxylated factor IX unreaotive with antibodies specific for the native structure but with the NH2-terminus of mature factor IX. In order to assess the universality of these observations we have recently cloned human prothrombin cDNA and expressed the gene in the same Chinese hamster ovary cell system used for factor IX. In contrast to factor IX, at low levels ofexpressionof the prothrombin gene, the prothrombin is fully carboxylated relative to a plasma prothrombin standard.The recombinant prothrombin exhibits the same specific clotting activity as plasma derivedprothrombin and is fully native as evaluated by conformation specific antibodies. At high levels of expression the capacityof the cells to carboxylate prothrombin can be exceeded leading to secretion of under carboxylated prothrombin. However, the absolute amount of fully carboxylated prothrombin that can be produced in this system appears to be a least fivefold greater that the absolute amount of highly carboxylated factor IX that can be synthesized.The elimination of carboxylation observed upon mutation of the propiece of factor IX suggest that the propiece contains a recognition element required for carboxylation of the protein. Assignment of a functional role to the propiece of factor IX represents the first determination of function for any pro sequence. It is anticipated that extension of these studies to prothrombin will demonstrate that this recognition signal is used by all the members of this class of proteins. In order to determine if the propiece is sufficient to designate a protein for gamma-carboxylation we are currently constructing chimeric proteins incorporating the propieceof prothrombin into the cDNA of normally uncarboxylated proteins.
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