Gotowe bibliografie tematyczne / Novel nucleolar protein

Gotowa bibliografia na temat „Novel nucleolar protein”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 20 lutego 2023

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Artykuły w czasopismach na temat "Novel nucleolar protein"

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Savino, T. M., R. Bastos, E. Jansen i D. Hernandez-Verdun. "The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis". Journal of Cell Science 112, nr 12 (15.06.1999): 1889–900. http://dx.doi.org/10.1242/jcs.112.12.1889.

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We report the molecular characterization of a novel nucleolar protein, Nop52, and its subcellular distribution during the cell cycle and nucleologenesis. This protein was originally identified with human autoantibodies which were subsequently used to clone its corresponding cDNA. Transfection experiments in mammalian cells have confirmed that this cDNA encodes a nucleolar protein that accumulates in the nucleoli and at the periphery of the chromosomes. Nop52 is the putative human homologue of the yeast ribosomal RNA processing protein RRP1 which is involved in pre-rRNA processing from 27S to 25S and 5.8S. In nucleoli, Nop52 is excluded from the ribosomal RNA transcription sites, accumulates in the granular external domain and mainly colocalizes with nucleolar proteins involved in the late processing step such as hPop1 and protein B23. During the building process of the nucleolus at the end of mitosis, a sequential order was observed in the assembly of nucleolar proteins of early and late processing mainly via the prenucleolar body pathway. The order is the following: fibrillarin, nucleolin, Nop52 together with protein B23 in the prenucleolar bodies, and simultaneously with hPop1, and finally Ki-67. The evolutionary conservation of Nop52 and the lethal effects observed in gene disruption experiments, predict a critical role for Nop52 in the generation of 28S rRNA.
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Pendle, Alison F., Gillian P. Clark, Reinier Boon, Dominika Lewandowska, Yun Wah Lam, Jens Andersen, Matthias Mann, Angus I. Lamond, John W. S. Brown i Peter J. Shaw. "Proteomic Analysis of the Arabidopsis Nucleolus Suggests Novel Nucleolar Functions". Molecular Biology of the Cell 16, nr 1 (styczeń 2005): 260–69. http://dx.doi.org/10.1091/mbc.e04-09-0791.

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The eukaryotic nucleolus is involved in ribosome biogenesis and a wide range of other RNA metabolism and cellular functions. An important step in the functional analysis of the nucleolus is to determine the complement of proteins of this nuclear compartment. Here, we describe the first proteomic analysis of plant (Arabidopsis thaliana) nucleoli, in which we have identified 217 proteins. This allows a direct comparison of the proteomes of an important nuclear structure between two widely divergent species: human and Arabidopsis. The comparison identified many common proteins, plant-specific proteins, proteins of unknown function found in both proteomes, and proteins that were nucleolar in plants but nonnucleolar in human. Seventy-two proteins were expressed as GFP fusions and 87% showed nucleolar or nucleolar-associated localization. In a striking and unexpected finding, we have identified six components of the postsplicing exon-junction complex (EJC) involved in mRNA export and nonsense-mediated decay (NMD)/mRNA surveillance. This association was confirmed by GFP-fusion protein localization. These results raise the possibility that in plants, nucleoli may have additional functions in mRNA export or surveillance.
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Fujimura, Akiko, Yuki Hayashi, Kazashi Kato, Yuichiro Kogure, Mutsuro Kameyama, Haruka Shimamoto, Hiroaki Daitoku, Akiyoshi Fukamizu, Toru Hirota i Keiji Kimura. "Identification of a novel nucleolar protein complex required for mitotic chromosome segregation through centromeric accumulation of Aurora B". Nucleic Acids Research 48, nr 12 (1.06.2020): 6583–96. http://dx.doi.org/10.1093/nar/gkaa449.

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Abstract The nucleolus is a membrane-less nuclear structure that disassembles when cells undergo mitosis. During mitosis, nucleolar factors are thus released from the nucleolus and dynamically change their subcellular localization; however, their functions remain largely uncharacterised. Here, we found that a nucleolar factor called nucleolar protein 11 (NOL11) forms a protein complex with two tryptophan-aspartic acid (WD) repeat proteins named WD-repeat protein 43 (WDR43) and Cirhin in mitotic cells. This complex, referred to here as the NWC (NOL11-WDR43-Cirhin) complex, exists in nucleoli during interphase and translocates to the periphery of mitotic chromosomes, i.e., perichromosomal regions. During mitotic progression, both the congression of chromosomes to the metaphase plate and sister chromatid cohesion are impaired in the absence of the NWC complex, as it is required for the centromeric enrichment of Aurora B and the associating phosphorylation of histone H3 at threonine 3. These results reveal the characteristics of a novel protein complex consisting of nucleolar proteins, which is required for regulating kinetochores and centromeres to ensure faithful chromosome segregation.
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Smith, Corey L., Timothy D. Matheson, Daniel J. Trombly, Xiaoming Sun, Eric Campeau, Xuemei Han, John R. Yates i Paul D. Kaufman. "A separable domain of the p150 subunit of human chromatin assembly factor-1 promotes protein and chromosome associations with nucleoli". Molecular Biology of the Cell 25, nr 18 (15.09.2014): 2866–81. http://dx.doi.org/10.1091/mbc.e14-05-1029.

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Chromatin assembly factor-1 (CAF-1) is a three-subunit protein complex conserved throughout eukaryotes that deposits histones during DNA synthesis. Here we present a novel role for the human p150 subunit in regulating nucleolar macromolecular interactions. Acute depletion of p150 causes redistribution of multiple nucleolar proteins and reduces nucleolar association with several repetitive element–containing loci. Of note, a point mutation in a SUMO-interacting motif (SIM) within p150 abolishes nucleolar associations, whereas PCNA or HP1 interaction sites within p150 are not required for these interactions. In addition, acute depletion of SUMO-2 or the SUMO E2 ligase Ubc9 reduces α-satellite DNA association with nucleoli. The nucleolar functions of p150 are separable from its interactions with the other subunits of the CAF-1 complex because an N-terminal fragment of p150 (p150N) that cannot interact with other CAF-1 subunits is sufficient for maintaining nucleolar chromosome and protein associations. Therefore these data define novel functions for a separable domain of the p150 protein, regulating protein and DNA interactions at the nucleolus.
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Westendorf, Joanne M., Konstantin N. Konstantinov, Steven Wormsley, Mei-Di Shu, Naoko Matsumoto-Taniura, Fabienne Pirollet, F. George Klier, Larry Gerace i Susan J. Baserga. "M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component". Molecular Biology of the Cell 9, nr 2 (luty 1998): 437–49. http://dx.doi.org/10.1091/mbc.9.2.437.

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We have previously developed a novel technique for isolation of cDNAs encoding M phase phosphoproteins (MPPs). In the work described herein, we further characterize MPP10, one of 10 novel proteins that we identified, with regard to its potential nucleolar function. We show that by cell fractionation, almost all MPP10 was found in isolated nucleoli. By immunofluorescence, MPP10 colocalized with nucleolar fibrillarin and other known nucleolar proteins in interphase cells but was not detected in the coiled bodies stained for either fibrillarin or p80 coilin, a protein found only in the coiled body. When nucleoli were separated into fibrillar and granular domains by treatment with actinomycin D, almost all the MPP10 was found in the fibrillar caps, which contain proteins involved in rRNA processing. In early to middle M phase of the cell cycle, MPP10 colocalized with fibrillarin to chromosome surfaces. At telophase, MPP10 was found in cellular structures that resembled nucleolus-derived bodies and prenucleolar bodies. Some of these bodies lacked fibrillarin, a previously described component of nucleolus-derived bodies and prenucleolar bodies, however, and the bulk of MPP10 arrived at the nucleolus later than fibrillarin. To further examine the properties of MPP10, we immunoprecipitated it from cell sonicates. The resulting precipitates contained U3 small nucleolar RNA (snoRNA) but no significant amounts of other box C/D snoRNAs. This association of MPP10 with U3 snoRNA was stable to 400 mM salt and suggested that MPP10 is a component of the human U3 small nucleolar ribonucleoprotein.
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Eilbracht, Jens, Michaela Reichenzeller, Michaela Hergt, Martina Schnölzer, Hans Heid, Michael Stöhr, Werner W. Franke i Marion S. Schmidt-Zachmann. "NO66, a Highly Conserved Dual Location Protein in the Nucleolus and in a Special Type of Synchronously Replicating Chromatin". Molecular Biology of the Cell 15, nr 4 (kwiecień 2004): 1816–32. http://dx.doi.org/10.1091/mbc.e03-08-0623.

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It has recently become clear that the nucleolus, the most prominent nuclear subcompartment, harbors diverse functions beyond its classic role in ribosome biogenesis. To gain insight into nucleolar functions, we have purified amplified nucleoli from Xenopus laevis oocytes using a novel approach involving fluorescence-activated cell sorting techniques. The resulting protein fraction was analyzed by mass spectrometry and used for the generation of monoclonal antibodies directed against nucleolar components. Here, we report the identification and molecular characterization of a novel, ubiquitous protein, which in most cell types appears to be a constitutive nucleolar component. Immunolocalization studies have revealed that this protein, termed NO66, is highly conserved during evolution and shows in most cells analyzed a dual localization pattern, i.e., a strong enrichment in the granular part of nucleoli and in distinct nucleoplasmic entities. Colocalizations with proteins Ki-67, HP1α, and PCNA, respectively, have further shown that the staining pattern of NO66 overlaps with certain clusters of late replicating chromatin. Biochemical experiments have revealed that protein NO66 cofractionates with large preribosomal particles but is absent from cytoplasmic ribosomes. We propose that in addition to its role in ribosome biogenesis protein NO66 has functions in the replication or remodeling of certain heterochromatic regions.
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Park, J. H., B. C. Jensen, C. T. Kifer i M. Parsons. "A novel nucleolar G-protein conserved in eukaryotes". Journal of Cell Science 114, nr 1 (1.01.2001): 173–85. http://dx.doi.org/10.1242/jcs.114.1.173.

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We describe here a novel, evolutionarily conserved set of predicted G-proteins. The founding member of this family, TbNOG1, was identified in a two-hybrid screen as a protein that interacts with NOPP44/46, a nucleolar phosphoprotein of Trypanosoma brucei. The biological relevance of the interaction was verified by co-localization and co-immunoprecipitation. TbNOG1 localized to the trypanosome nucleolus and interacted with domains of NOPP44/46 that are found in several other nucleolar proteins. Genes encoding proteins highly related to TbNOG1 are present in yeast and metazoa, and related G domains are found in bacteria. We show that NOG1 proteins in humans and Saccharomyces cerevisae are also nucleolar. The S. cerevisae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. Together these data suggest that NOG1 may play an important role in nucleolar functions. The GTP-binding region of TbNOG1 is similar to those of Obg and DRG proteins, which, together with NOG, form a newly recognized family of G-proteins, herein named ODN. The ODN family differs significantly from other G-protein families, and shows several diagnostic sequence characteristics. All organisms appear to possess an ODN gene, pointing to the biological significance of this family of G-proteins.
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Kadowaki, T., R. Schneiter, M. Hitomi i A. M. Tartakoff. "Mutations in nucleolar proteins lead to nucleolar accumulation of polyA+ RNA in Saccharomyces cerevisiae." Molecular Biology of the Cell 6, nr 9 (wrzesień 1995): 1103–10. http://dx.doi.org/10.1091/mbc.6.9.1103.

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Synthesis of mRNA and rRNA occur in the chromatin-rich nucleoplasm and the nucleolus, respectively. Nevertheless, we here report that a Saccharomyces cerevisiae gene, MTR3, previously implicated in mRNA transport, codes for a novel essential 28-kDa nucleolar protein. Moreover, in mtr3-1 the accumulated polyA+ RNA actually colocalizes with nucleolar antigens, the nucleolus becomes somewhat disorganized, and rRNA synthesis and processing are inhibited. A strain with a ts conditional mutation in RNA polymerase I also shows nucleolar accumulation of polyA+ RNA, whereas strains with mutations in the nucleolar protein Nop1p do not. Thus, in several mutant backgrounds, when mRNA cannot be exported i concentrates in the nucleolus. mRNA may normally encounter nucleolar components before export and proteins such as Mtr3p may be critical for export of both mRNA and ribosomal subunits.
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Damianov, Andrey, Michael Kann, William S. Lane i Albrecht Bindereif. "Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs". Biological Chemistry 387, nr 10/11 (1.10.2006): 1455–60. http://dx.doi.org/10.1515/bc.2006.182.

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Abstract The biogenesis of spliceosomal small nuclear RNAs (snRNAs) involves organized translocations between the cytoplasm and certain nuclear domains, such as Cajal bodies and nucleoli. Here we identify human RBM28 protein as a novel snRNP component, based on affinity selection of U6 small nuclear ribonucleoprotein (snRNP). As shown by immunofluorescence, RBM28 is a nucleolar protein. Anti-RBM28 immunoprecipitation from HeLa cell lysates revealed that this protein specifically associates with U1, U2, U4, U5, and U6 snRNAs. Our data provide the first evidence that RBM28 is a common nucleolar component of the spliceosomal ribonucleoprotein complexes, possibly coordinating their transition through the nucleolus.
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Brown, Isabella N., M. Carmen Lafita-Navarro i Maralice Conacci-Sorrell. "Regulation of Nucleolar Activity by MYC". Cells 11, nr 3 (7.02.2022): 574. http://dx.doi.org/10.3390/cells11030574.

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The nucleolus harbors the machinery necessary to produce new ribosomes which are critical for protein synthesis. Nucleolar size, shape, and density are highly dynamic and can be adjusted to accommodate ribosome biogenesis according to the needs for protein synthesis. In cancer, cells undergo continuous proliferation; therefore, nucleolar activity is elevated due to their high demand for protein synthesis. The transcription factor and universal oncogene MYC promotes nucleolar activity by enhancing the transcription of ribosomal DNA (rDNA) and ribosomal proteins. This review summarizes the importance of nucleolar activity in mammalian cells, MYC’s role in nucleolar regulation in cancer, and discusses how a better understanding (and the potential inhibition) of aberrant nucleolar activity in cancer cells could lead to novel therapeutics.
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Rozprawy doktorskie na temat "Novel nucleolar protein"

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Utama, B. "Isolation and characterization of Nrap, a novel nucleolar protein /". [St. Lucia, Qld.], 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16281.pdf.

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Inder, Kerry, i n/a. "The Functional Role of NRAP in the Nucleolus". Griffith University. School of Biomolecular and Biomedical Science, 2006. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20070201.133347.

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The nucleolus is the site for rRNA synthesis, a process requiring the recruitment of many proteins involved in ribosomal biogenesis. Nrap is a novel nucleolar protein found to be present in all eukaryotes. Preliminary characterisation of Nrap suggested it was likely to participate in ribosome biogenesis but as with many other nucleolar proteins, the functional role of Nrap is largely unknown. In this study, the role of mammalian Nrap in the nucleolus and in ribosome biogenesis was explored. Initially, a number of tools were generated to investigate Nrap function. This involved raising and purifying a polyclonal antibody against the N-terminal region of Nrap. The anti-Nrap antibody was found to detect two Nrap bands in mouse fibroblast cells, possibly corresponding to the two mouse Nrap isoforms, and . In addition, mammalian expression vectors containing the full Nrap sequence as well as deletion constructs were created. The subcellular localisation of each construct was observed by fluorescent microscopy. It was revealed that recombinant Nrap did not localise to the nucleolus, possibly because it was exported to undergo degradation by the 26S proteasome. Two putative NLSs were found to be responsible for directing Nrap to the nucleus but a region accountable for nucleolar localisation was not identified. The data indicated that multiple domains working together are likely to direct Nrap to the nucleolus. Nrap was also observed to co-localise with nucleolar proteins B23 and p19ARF. Moreover, it was shown by reciprocal immunoprecipitation that these three nucleolar proteins existed in a complex in unsynchronised mouse fibroblast cells. Recent reports demonstrated a complex relationship between B23 and p19ARF although the functional significance remained unclear. Nrap's in vivo association with B23 and p19ARF indicated a specific functional role in the nucleolus. Nrap knockdown using siRNA significantly increased B23 protein levels in a dose-dependent manner and down-regulated p19ARF protein levels at higher siRNA concentration. Preliminary studies also implicated Nrap in cell proliferation through these novel interactions. Both endogenous and recombinant Nrap were found to be highly unstable suggesting that Nrap might regulate B23 and p19ARF through its own tightly regulated stability. Finally, the role of Nrap in rRNA processing was investigated by northern blot analysis. Nrap knockdown was found to affect the levels of 45S, 32S and 28S rRNAs. The changes found may be a consequence of the concurrent perturbation in the levels of B23 and p19ARF caused by Nrap knockdown. As the results were not consistent with previous reports, it was likely that changes to rRNA processing could be contributed to Nrap loss of function. This study demonstrated for the first time a functional role of Nrap in rRNA processing possibly through its association with B23 and p19ARF.
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Inder, Kerry. "The Functional Role of NRAP in the Nucleolus". Thesis, Griffith University, 2006. http://hdl.handle.net/10072/367738.

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The nucleolus is the site for rRNA synthesis, a process requiring the recruitment of many proteins involved in ribosomal biogenesis. Nrap is a novel nucleolar protein found to be present in all eukaryotes. Preliminary characterisation of Nrap suggested it was likely to participate in ribosome biogenesis but as with many other nucleolar proteins, the functional role of Nrap is largely unknown. In this study, the role of mammalian Nrap in the nucleolus and in ribosome biogenesis was explored. Initially, a number of tools were generated to investigate Nrap function. This involved raising and purifying a polyclonal antibody against the N-terminal region of Nrap. The anti-Nrap antibody was found to detect two Nrap bands in mouse fibroblast cells, possibly corresponding to the two mouse Nrap isoforms, and . In addition, mammalian expression vectors containing the full Nrap sequence as well as deletion constructs were created. The subcellular localisation of each construct was observed by fluorescent microscopy. It was revealed that recombinant Nrap did not localise to the nucleolus, possibly because it was exported to undergo degradation by the 26S proteasome. Two putative NLSs were found to be responsible for directing Nrap to the nucleus but a region accountable for nucleolar localisation was not identified. The data indicated that multiple domains working together are likely to direct Nrap to the nucleolus. Nrap was also observed to co-localise with nucleolar proteins B23 and p19ARF. Moreover, it was shown by reciprocal immunoprecipitation that these three nucleolar proteins existed in a complex in unsynchronised mouse fibroblast cells. Recent reports demonstrated a complex relationship between B23 and p19ARF although the functional significance remained unclear. Nrap's in vivo association with B23 and p19ARF indicated a specific functional role in the nucleolus. Nrap knockdown using siRNA significantly increased B23 protein levels in a dose-dependent manner and down-regulated p19ARF protein levels at higher siRNA concentration. Preliminary studies also implicated Nrap in cell proliferation through these novel interactions. Both endogenous and recombinant Nrap were found to be highly unstable suggesting that Nrap might regulate B23 and p19ARF through its own tightly regulated stability. Finally, the role of Nrap in rRNA processing was investigated by northern blot analysis. Nrap knockdown was found to affect the levels of 45S, 32S and 28S rRNAs. The changes found may be a consequence of the concurrent perturbation in the levels of B23 and p19ARF caused by Nrap knockdown. As the results were not consistent with previous reports, it was likely that changes to rRNA processing could be contributed to Nrap loss of function. This study demonstrated for the first time a functional role of Nrap in rRNA processing possibly through its association with B23 and p19ARF.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
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Ho, Joseph Tsung-yo. "Bridging cell growth and proliferation : identification and characterization of binding partners for pescadillo, a novel nucleolar protein involved in tumorigenesis and DNA damage /". Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/10659.

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Bai, Qi Yun, i 白其昀. "Expression of a novel highly phosphorylated human nucleolar protein pl30 is proliferation-associated: identification of the cDNAS, Alterations during cell-cycle and correlation to the nucleologenesis". Thesis, 1995. http://ndltd.ncl.edu.tw/handle/24607301009942442654.

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Tsai, Wen-Hai, i 蔡文海. "Biochemical and Molecular Biological Characterizations of Nucleolin and a Novel PHD-finger Protein". Thesis, 1999. http://ndltd.ncl.edu.tw/handle/93349080846838181301.

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博士
國立臺灣大學
分子醫學研究所
87
Maintenance of chromosome integrity is a fundamental requirement in all-living organisms. Genes are expressed in a temporal or tissue-specific manner or activated in response to extracellular stimuli. Gene expression can be tightly controlled at several levels, including transcriptional, post-transcriptional (mRNA processing and transport), translational (protein synthesis) and post-translational levels (glycosylation or phosphorylation etc.). For most genes transcriptional controls are paramount. The initiation of transcription in eukaryotes is a highly and tightly controlled process. Genes exist at some time in an inert state that was tightly packaged with histones in to chromatin. Before transcription can occur, this inert structure must be decondensed so that transcriptional control sequences are made available to regulatory proteins. Once decondensation of chromatin has occurred, the scene is set for the second activation steps: the interaction of regulatory proteins, commonly referred to as transcription factors or trans-acting factors, with specific DNA sequences. Such interactions of these bound factors with general transcription factors mediate gene transcription. Protein-protein interaction and posttranslational modifications are important for regulating activities of these trans-acting factors. There are two models for the initiation of transcription by RNA pol II : the stepwise assembly model and the holoenzyme model. The conventional model (stepwise assembly model) for ordered transcriptional initiation by RNA pol II is characterized by a distinct series of events : (1) recognition of core promoter elements by TFIID, (2) recognition of the TFIID-promoter complex by TFIIB and TFIIA, (3) recruitment of the TFIIF/pol II complex, (4) binding of TFIIE and TFIIH to complete the preinitiation complex, (5) promoter melting and formation of an "open" initiation complex, (6) synthesis of the nascent mRNA transcript, (7) release of pol II contact with the promoter ("promoter clearance"), and (8) elongation of the RNA transcript. Recently, the discovery that a subset of the GTFs (General Transcription Factor) exists in a preassembled form in an RNA pol II holoenzyme, suggests that the majority of the initiation machinery can bind to a promoter in a single step (RNA pol II holoenzyme model). The assembly of the GTFs is subject to regulation by activator and repressor proteins. Activators can recruit GTFs to a promoter, thereby accelerating the assembly process, whereas repressor proteins can inhibit transcription by blocking the assembly of GTFs. The mechanism of activator can function during multiple stages of transcription. These include (1) removal of repressor molecules from promoter DNA, (2) recruitment of GTFs and pol II to a promoter, (3) induction of conformation changes in the preinitiation complex, (4) induction of covalent modification of proteins in the preinitiation complex, and (5) stimulation of promoter clearance and elongation. These steps involve direct interactions between activators and GTFs. The condensation of eukaryotic DNA in chromatin functions not only to constrain the genome within the boundaries of the cell nucleus but also to suppress gene activity in a general manner. PHD-finger domain, a zinc finger-like motif, has a unique Cys4-His-Cys3 pattern, spanning approximately 50-80 residues. Generally the PHD-fingers are protein-protein interaction domains or that they recognize a set of similar nuclear targets related to chromatin structure and chromatin regulation, such as the differentially modified tails of the nucleosomal histones. We used the alpha-1 acid glycoprotein (AGP) gene as a model for studying transcriptional regulation. AGP is an acute responsive, liver-specific gene. Its expression is regulated by both positive and negative trans-acting factors. At least five cis elements have been identified within the 180-bp region of AGP promoter. Four of these sites, A, C, D and E are recognized by AGP/EBP or AGB/EBP-like factors in liver nuclear extracts. A, C, D and E regions are positive regulatory elements enhancing the expression of AGP gene while B motif is negative regulatory element repressing the expression of AGP gene. There are two parts in this thesis : (1) Biochemical purification and characterization of the negative transcription factors for AGP gene expression. The purified factor has been identified as nucleolin by amino acid analysis. Furthermore, we show that nucleolin can function as a transcription repressor for the AGP gene. (2) Identification, molecular cloning and biological characterization of a novel PHD-finger protein DPKAP (DNA-PK Activating Protein). DPKAP interacts with DNA-PK physically and functionally. DPKAP stimulates the DNA-PK kinase activity in vitro. Genetic evidence strongly suggests for the crucial role of DNA-PK in DNA double-strand break (DSB) repair and V(D)J recombination. However, the precise regulatory mechanism of DNA-PK in these processes remains to be elucidated. The potential in vivo functions of DPKAP on DNA DSB repair and V(D)J recombination remain to be investigated.
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Części książek na temat "Novel nucleolar protein"

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Asea, Alexzander, Appukuttan R. Pradeep i Punit Kaur. "Nucleolin: A Novel Intracellular Transporter of HSPA1A". W Heat Shock Proteins, 115–24. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4740-1_8.

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A Becker-Kojić, Zorica, José Manuel García-Verdugo, Anne-Kathrin Schott, Vicente Herranz-Pérez, Ivan Zipančić i Vicente Hernández-Rabaza. "Membrane-to-Nucleus Signaling in Human Blood Progenitor Cells Reveals an Efficient GM-Free Reprogramming to Pluripotency". W Stem Cell Research [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.108950.

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The generation of induced pluripotent stem cells (iPSCs) by forced expression of defined transcription factors has revolutionized regenerative medicine. These cells have similar features to embryonic stem cells (ESCs) regarding self-renewal and their ability to differentiate into any cell type in the body. In spite of many improvements, in using nonviral delivery reprogramming methods, there are still challenges to overcome regarding safety before patient-made iPSCs can be used in regular clinical practice. We have recently reported about a gene manipulation-free method of generating human pluripotent stem cells (PSCs), based on activation of the novel human GPI-linked glycoprotein ACA. The process of dedifferentiation of blood progenitor cells that leads to the generation of blood-derived pluripotent stem cells (BD-PSCs) is initiated upon cross-linking of this protein via activation of PLCγ/PI3K/Akt pathway. These cells are mortal, express pluripotent markers, and redifferentiate in vitro into cells of all three germ layers. The ultrastructural analysis of BD-PSCs, by means of electron microscopy, revealed them similar to human ESCs with large dense nucleolus and scarce cytoplasm. BD-PSCs are autologous stem cells and while nonteratogenic offer a new alternative that overcomes immunological, ethical, and safety concerns and opens up a new avenue in treating contemporarily intractable diseases and generally in human therapeutics.
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Streszczenia konferencji na temat "Novel nucleolar protein"

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Demokan, Semra, Alice Y. Chuang, Kavita M. Pattani, David Sidransky, Wayne Koch i Joseph A. Califano. "Abstract 666: Validation of nucleolar protein 4 as a novel methylated tumor suppressor gene in head and neck cancer." W 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.am2013-666.

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Chiara, Brignole, Veronica Bensa, Genny Del Zotto, Silvia Bruno, Nuno A. Fonseca, Ana F. Cruz, Daniela Di Paolo i in. "Abstract A101: Nucleolin: A novel cell surface protein for neuroblastoma targeted therapy". W Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-a101.

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Wu, Guanhui, Buket Onel i Danzhou Yang. "Abstract 1474: Identifying novel chromatin binding sites of nucleolin protein in cancer cells". W Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1474.

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Raporty organizacyjne na temat "Novel nucleolar protein"

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Paik, Jason C. The Role of a Novel Nucleolar Protein in Regulation of E2F1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, wrzesień 2009. http://dx.doi.org/10.21236/ada525619.

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