Base de dados : MEDLINE
Pesquisa : A11.284.430.106.279.345.190.160.180.625 [Categoria DeCS]
Referências encontradas : 8562 [refinar]
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[PMID]:29212533
[Au] Autor:Gutiérrez G; Millán-Zambrano G; Medina DA; Jordán-Pla A; Pérez-Ortín JE; Peñate X; Chávez S
[Ad] Endereço:Departamento de Genética, Universidad de Sevilla, Seville, Spain.
[Ti] Título:Subtracting the sequence bias from partially digested MNase-seq data reveals a general contribution of TFIIS to nucleosome positioning.
[So] Source:Epigenetics Chromatin;10(1):58, 2017 12 07.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: TFIIS stimulates RNA cleavage by RNA polymerase II and promotes the resolution of backtracking events. TFIIS acts in the chromatin context, but its contribution to the chromatin landscape has not yet been investigated. Co-transcriptional chromatin alterations include subtle changes in nucleosome positioning, like those expected to be elicited by TFIIS, which are elusive to detect. The most popular method to map nucleosomes involves intensive chromatin digestion by micrococcal nuclease (MNase). Maps based on these exhaustively digested samples miss any MNase-sensitive nucleosomes caused by transcription. In contrast, partial digestion approaches preserve such nucleosomes, but introduce noise due to MNase sequence preferences. A systematic way of correcting this bias for massively parallel sequencing experiments is still missing. RESULTS: To investigate the contribution of TFIIS to the chromatin landscape, we developed a refined nucleosome-mapping method in Saccharomyces cerevisiae. Based on partial MNase digestion and a sequence-bias correction derived from naked DNA cleavage, the refined method efficiently mapped nucleosomes in promoter regions rich in MNase-sensitive structures. The naked DNA correction was also important for mapping gene body nucleosomes, particularly in those genes whose core promoters contain a canonical TATA element. With this improved method, we analyzed the global nucleosomal changes caused by lack of TFIIS. We detected a general increase in nucleosomal fuzziness and more restricted changes in nucleosome occupancy, which concentrated in some gene categories. The TATA-containing genes were preferentially associated with decreased occupancy in gene bodies, whereas the TATA-like genes did so with increased fuzziness. The detected chromatin alterations correlated with functional defects in nascent transcription, as revealed by genomic run-on experiments. CONCLUSIONS: The combination of partial MNase digestion and naked DNA correction of the sequence bias is a precise nucleosomal mapping method that does not exclude MNase-sensitive nucleosomes. This method is useful for detecting subtle alterations in nucleosome positioning produced by lack of TFIIS. Their analysis revealed that TFIIS generally contributed to nucleosome positioning in both gene promoters and bodies. The independent effect of lack of TFIIS on nucleosome occupancy and fuzziness supports the existence of alternative chromatin dynamics during transcription elongation.
[Mh] Termos MeSH primário: Nuclease do Micrococo/metabolismo
Nucleossomos/metabolismo
Fatores de Elongação da Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequenciamento de Nucleotídeos em Larga Escala
Reação em Cadeia da Polimerase em Tempo Real
Saccharomyces cerevisiae/metabolismo
Técnica de Subtração
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleosomes); 0 (Transcriptional Elongation Factors); 0 (transcription factor S-II); EC 3.1.31.1 (Micrococcal Nuclease)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0165-x


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[PMID]:29339721
[Au] Autor:Kilic S; Felekyan S; Doroshenko O; Boichenko I; Dimura M; Vardanyan H; Bryan LC; Arya G; Seidel CAM; Fierz B
[Ad] Endereço:Laboratory of Biophysical Chemistry of Macromolecules, Institute of Chemical Sciences and Engineering (ISIC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
[Ti] Título:Single-molecule FRET reveals multiscale chromatin dynamics modulated by HP1α.
[So] Source:Nat Commun;9(1):235, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The dynamic architecture of chromatin fibers, a key determinant of genome regulation, is poorly understood. Here, we employ multimodal single-molecule Förster resonance energy transfer studies to reveal structural states and their interconversion kinetics in chromatin fibers. We show that nucleosomes engage in short-lived (micro- to milliseconds) stacking interactions with one of their neighbors. This results in discrete tetranucleosome units with distinct interaction registers that interconvert within hundreds of milliseconds. Additionally, we find that dynamic chromatin architecture is modulated by the multivalent architectural protein heterochromatin protein 1α (HP1α), which engages methylated histone tails and thereby transiently stabilizes stacked nucleosomes. This compacted state nevertheless remains dynamic, exhibiting fluctuations on the timescale of HP1α residence times. Overall, this study reveals that exposure of internal DNA sites and nucleosome surfaces in chromatin fibers is governed by an intrinsic dynamic hierarchy from micro- to milliseconds, allowing the gene regulation machinery to access compact chromatin.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Transferência Ressonante de Energia de Fluorescência/métodos
Nucleossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatina/química
Cromatina/genética
DNA/química
DNA/genética
DNA/metabolismo
Regulação da Expressão Gênica
Histonas/metabolismo
Cinética
Metilação
Microscopia de Fluorescência
Conformação Molecular
Conformação de Ácido Nucleico
Nucleossomos/química
Nucleossomos/genética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Histones); 0 (Nucleosomes); 107283-02-3 (heterochromatin-specific nonhistone chromosomal protein HP-1); 9007-49-2 (DNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02619-5


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[PMID]:29339748
[Au] Autor:Lee S; Oh S; Jeong K; Jo H; Choi Y; Seo HD; Kim M; Choe J; Kwon CS; Lee D
[Ad] Endereço:Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
[Ti] Título:Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.
[So] Source:Nat Commun;9(1):240, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2-Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.
[Mh] Termos MeSH primário: Chaperonas de Histonas/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Proteínas Nucleares/metabolismo
Nucleossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cromatina/genética
Cromatina/metabolismo
Regulação Fúngica da Expressão Gênica
Chaperonas de Histonas/genética
Histona-Lisina N-Metiltransferase/genética
Histonas/metabolismo
Lisina/metabolismo
Mutação
Proteínas Nucleares/genética
Nucleossomos/genética
Ligação Proteica
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Histone Chaperones); 0 (Histones); 0 (Nuclear Proteins); 0 (Nucleosomes); 0 (Saccharomyces cerevisiae Proteins); EC 2.1.1.43 (Dot1 protein, S cerevisiae); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02759-8


  4 / 8562 MEDLINE  
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[PMID]:29368470
[Au] Autor:Mazina MY; Vorobyeva NE
[Ti] Título:[The role of ATP-dependent chromatin remodeling complexes in regulation of genetic processes].
[So] Source:Genetika;52(5):529-40, 2016 May.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Compaction of the genomic DNA into the chromatin structure reduces the accessibility of DNAbinding protein sites and complicates the realization of replication and transcription. In the cell, the negative effects of DNA condensation into chromatin are overcome by recruiting the complexes that change the chromatin structure and are involved in the regulation of transcription and replication. The chromatin remodeling process includes the alteration of nucleosome position and chromatin density and changes in the histone composition of the nucleosomes. ATP-dependent chromatin remodeling is performed by enzymes­chromatin remodeling complexes. The united activity of these enzymes forms the dynamic properties of chromatin during different nuclear processes such as transcription, replication, DNA repair, homological recombination, and chromatin assembly. In this review, we summarize the currently available data on the structure of chromatin remodeling complexes of different families, the pathways of their recruitment to certain chromatin sites, and their functional activity.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Montagem e Desmontagem da Cromatina/fisiologia
Nucleossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Reparo do DNA/fisiologia
Replicação do DNA/fisiologia
Recombinação Homóloga/fisiologia
Seres Humanos
Nucleossomos/genética
Transcrição Genética/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Nucleosomes); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  5 / 8562 MEDLINE  
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[PMID]:29284710
[Au] Autor:Hauer MH; Gasser SM
[Ad] Endereço:Friedrich Miescher Institute for Biomedical Research, CH-4058 Basel, Switzerland.
[Ti] Título:Chromatin and nucleosome dynamics in DNA damage and repair.
[So] Source:Genes Dev;31(22):2204-2221, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chromatin is organized into higher-order structures that form subcompartments in interphase nuclei. Different categories of specialized enzymes act on chromatin and regulate its compaction and biophysical characteristics in response to physiological conditions. We present an overview of the function of chromatin structure and its dynamic changes in response to genotoxic stress, focusing on both subnuclear organization and the physical mobility of DNA. We review the requirements and mechanisms that cause chromatin relocation, enhanced mobility, and chromatin unfolding as a consequence of genotoxic lesions. An intriguing link has been established recently between enhanced chromatin dynamics and histone loss.
[Mh] Termos MeSH primário: Cromatina/química
Cromatina/metabolismo
Dano ao DNA
Reparo do DNA
Nucleossomos/metabolismo
[Mh] Termos MeSH secundário: Histonas/metabolismo
Nucleossomos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (Nucleosomes)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1101/gad.307702.117


  6 / 8562 MEDLINE  
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[PMID]:29183721
[Au] Autor:Gupta MK; Agarawal M; Banu K; Reddy KS; Gaur D; Dhar SK
[Ad] Endereço:Special Centre for Molecular Medicine, Jawaharlal Nehru University, New Delhi, India.
[Ti] Título:Role of Chromatin assembly factor 1 in DNA replication of Plasmodium falciparum.
[So] Source:Biochem Biophys Res Commun;495(1):1285-1291, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleosome assembly in P. falciparum could be the key process in maintaining its genomic integrity as DNA replicates more than once per cell cycle during several stages of its life cycle. Here, we report the functional characterization of P. falciparum chromatin assembly factor 1 (CAF1), which interacts with several proteins namely PfCAF2, Histones, PfHP1 and others. Consistent with the above findings, we demonstrate the presence of PfCAF1 at the telomeric repeat regions, central and subtelomeric var genes of multiple var gene family along with PfHP1. Further, we report the upregulation of PfCAF1 after treatment with genotoxic agents like MMS and HU. Together, these findings establish role of PfCAF1 in heterochromatin maintenance and as histone chaperone in nucleosome assembly and DNA damage repair.
[Mh] Termos MeSH primário: Fator 1 de Modelagem da Cromatina/genética
Reparo do DNA/genética
Replicação do DNA/genética
DNA de Protozoário/genética
Nucleossomos/genética
Plasmodium falciparum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin Assembly Factor-1); 0 (DNA, Protozoan); 0 (Nucleosomes)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE


  7 / 8562 MEDLINE  
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[PMID]:29220652
[Au] Autor:Lehmann LC; Hewitt G; Aibara S; Leitner A; Marklund E; Maslen SL; Maturi V; Chen Y; van der Spoel D; Skehel JM; Moustakas A; Boulton SJ; Deindl S
[Ad] Endereço:Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124 Uppsala, Sweden.
[Ti] Título:Mechanistic Insights into Autoinhibition of the Oncogenic Chromatin Remodeler ALC1.
[So] Source:Mol Cell;68(5):847-859.e7, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human ALC1 is an oncogene-encoded chromatin-remodeling enzyme required for DNA repair that possesses a poly(ADP-ribose) (PAR)-binding macro domain. Its engagement with PARylated PARP1 activates ALC1 at sites of DNA damage, but the underlying mechanism remains unclear. Here, we establish a dual role for the macro domain in autoinhibition of ALC1 ATPase activity and coupling to nucleosome mobilization. In the absence of DNA damage, an inactive conformation of the ATPase is maintained by juxtaposition of the macro domain against predominantly the C-terminal ATPase lobe through conserved electrostatic interactions. Mutations within this interface displace the macro domain, constitutively activate the ALC1 ATPase independent of PARylated PARP1, and alter the dynamics of ALC1 recruitment at DNA damage sites. Upon DNA damage, binding of PARylated PARP1 by the macro domain induces a conformational change that relieves autoinhibitory interactions with the ATPase motor, which selectively activates ALC1 remodeling upon recruitment to sites of DNA damage.
[Mh] Termos MeSH primário: Montagem e Desmontagem da Cromatina
Dano ao DNA
DNA Helicases/metabolismo
Reparo do DNA
Proteínas de Ligação a DNA/metabolismo
Nucleossomos/enzimologia
[Mh] Termos MeSH secundário: Domínio Catalítico
Linhagem Celular Tumoral
DNA Helicases/química
DNA Helicases/genética
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
Ativação Enzimática
Seres Humanos
Microscopia Eletrônica
Simulação de Dinâmica Molecular
Mutação
Nucleossomos/química
Poli(ADP-Ribose) Polimerase-1/química
Poli(ADP-Ribose) Polimerase-1/metabolismo
Poli ADP Ribosilação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Espalhamento a Baixo Ângulo
Eletricidade Estática
Relação Estrutura-Atividade
Fatores de Tempo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Nucleosomes); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (CHD1L protein, human)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:29198523
[Au] Autor:Truong DM; Boeke JD
[Ad] Endereço:Institute for Systems Genetics, Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA. Electronic address: davemtruong@gmail.com.
[Ti] Título:Resetting the Yeast Epigenome with Human Nucleosomes.
[So] Source:Cell;171(7):1508-1519.e13, 2017 Dec 14.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Humans and yeast are separated by a billion years of evolution, yet their conserved histones retain central roles in gene regulation. Here, we "reset" yeast to use core human nucleosomes in lieu of their own (a rare event taking 20 days), which initially only worked with variant H3.1. The cells adapt by acquiring suppressor mutations in cell-division genes or by acquiring certain aneuploid states. Converting five histone residues to their yeast counterparts restored robust growth. We reveal that humanized nucleosomes are positioned according to endogenous yeast DNA sequence and chromatin-remodeling network, as judged by a yeast-like nucleosome repeat length. However, human nucleosomes have higher DNA occupancy, globally reduce RNA content, and slow adaptation to new conditions by delaying chromatin remodeling. These humanized yeasts (including H3.3) pose fundamental new questions about how chromatin is linked to many cell processes and provide a platform to study histone variants via yeast epigenome reprogramming.
[Mh] Termos MeSH primário: Histonas/química
Nucleossomos/química
Saccharomyces cerevisiae/química
[Mh] Termos MeSH secundário: Montagem e Desmontagem da Cromatina
RNA Polimerases Dirigidas por DNA/metabolismo
Regulação da Expressão Gênica
Células HeLa
Histonas/metabolismo
Seres Humanos
Mutação
Saccharomyces cerevisiae/metabolismo
Especificidade da Espécie
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Nucleosomes); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  9 / 8562 MEDLINE  
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[PMID]:29194442
[Au] Autor:Niina T; Brandani GB; Tan C; Takada S
[Ad] Endereço:Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan.
[Ti] Título:Sequence-dependent nucleosome sliding in rotation-coupled and uncoupled modes revealed by molecular simulations.
[So] Source:PLoS Comput Biol;13(12):e1005880, 2017 Dec.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:While nucleosome positioning on eukaryotic genome play important roles for genetic regulation, molecular mechanisms of nucleosome positioning and sliding along DNA are not well understood. Here we investigated thermally-activated spontaneous nucleosome sliding mechanisms developing and applying a coarse-grained molecular simulation method that incorporates both long-range electrostatic and short-range hydrogen-bond interactions between histone octamer and DNA. The simulations revealed two distinct sliding modes depending on the nucleosomal DNA sequence. A uniform DNA sequence showed frequent sliding with one base pair step in a rotation-coupled manner, akin to screw-like motions. On the contrary, a strong positioning sequence, the so-called 601 sequence, exhibits rare, abrupt transitions of five and ten base pair steps without rotation. Moreover, we evaluated the importance of hydrogen bond interactions on the sliding mode, finding that strong and weak bonds favor respectively the rotation-coupled and -uncoupled sliding movements.
[Mh] Termos MeSH primário: Montagem e Desmontagem da Cromatina
Histonas
Simulação de Dinâmica Molecular
Nucleossomos
[Mh] Termos MeSH secundário: Sequência de Bases
Biologia Computacional
Histonas/química
Histonas/genética
Histonas/metabolismo
Ligações de Hidrogênio
Modelos Genéticos
Nucleossomos/química
Nucleossomos/genética
Nucleossomos/metabolismo
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Nucleosomes)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005880


  10 / 8562 MEDLINE  
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[PMID]:28468903
[Au] Autor:Hodges AJ; Gloss LM; Wyrick JJ
[Ad] Endereço:School of Molecular Biosciences, Washington State University, Pullman, Washington 99164.
[Ti] Título:Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in .
[So] Source:Genetics;206(3):1339-1348, 2017 07.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The essential histone chaperone FACT plays a critical role in DNA replication, repair, and transcription, primarily by binding to histone H2A-H2B dimers and regulating their assembly into nucleosomes. While FACT histone chaperone activity has been extensively studied, the exact nature of the H2A and H2B residues important for FACT binding remains controversial. In this study, we characterized the functions of residues in the histone H2A and H2B acidic patch, which is important for binding many chromatin-associated factors. We found that mutations in essential acidic patch residues cause a defect in histone occupancy in yeast, even though most of these histone mutants are expressed normally in yeast and form stable nucleosomes Instead, we show that two acidic patch residues, H2B L109 and H2A E57, are important for histone binding to FACT We systematically screened mutants in other H2A and H2B residues previously suspected to be important for FACT binding and confirmed the importance of H2B M62 using an FACT-binding assay. Furthermore, we show that, like deletion mutants in FACT subunits, an H2A E57 and H2B M62 double mutant is lethal in yeast. In summary, we show that residues in the nucleosome acidic patch promote histone occupancy and are important for FACT binding to H2A-H2B dimers in yeast.
[Mh] Termos MeSH primário: Histonas/metabolismo
Nucleossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores de Transcrição/metabolismo
Fatores de Elongação da Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Histonas/genética
Proteína 1 de Modelagem do Nucleossomo/genética
Proteína 1 de Modelagem do Nucleossomo/metabolismo
Nucleossomos/química
Nucleossomos/genética
Ligação Proteica
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Transcrição/genética
Fatores de Elongação da Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Histones); 0 (NAP1 protein, S cerevisiae); 0 (Nucleosome Assembly Protein 1); 0 (Nucleosomes); 0 (POB3 protein, S cerevisiae); 0 (SPT16 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 0 (Transcriptional Elongation Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.117.201939



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde