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  1 / 6030 MEDLINE  
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[PMID]:29191233
[Au] Autor:Posukh OV; Maksimov DA; Laktionov PP; Koryakov DE; Belyakin SN
[Ad] Endereço:Genomics Lab, Institute of Molecular and Cellular Biology SB RAS, Lavrentyev ave. 8/2, Novosibirsk, Russia, 630090.
[Ti] Título:Functional dissection of Drosophila melanogaster SUUR protein influence on H3K27me3 profile.
[So] Source:Epigenetics Chromatin;10(1):56, 2017 12 01.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In eukaryotes, heterochromatin replicates late in S phase of the cell cycle and contains specific covalent modifications of histones. SuUR mutation found in Drosophila makes heterochromatin replicate earlier than in wild type and reduces the level of repressive histone modifications. SUUR protein was shown to be associated with moving replication forks, apparently through the interaction with PCNA. The biological process underlying the effects of SUUR on replication and composition of heterochromatin remains unknown. RESULTS: Here we performed a functional dissection of SUUR protein effects on H3K27me3 level. Using hidden Markow model-based algorithm we revealed SuUR-sensitive chromosomal regions that demonstrated unusual characteristics: They do not contain Polycomb and require SUUR function to sustain H3K27me3 level. We tested the role of SUUR protein in the mechanisms that could affect H3K27me3 histone levels in these regions. We found that SUUR does not affect the initial H3K27me3 pattern formation in embryogenesis or Polycomb distribution in the chromosomes. We also ruled out the possible effect of SUUR on histone genes expression and its involvement in DSB repair. CONCLUSIONS: Obtained results support the idea that SUUR protein contributes to the heterochromatin maintenance during the chromosome replication. A model that explains major SUUR-associated phenotypes is proposed.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Histonas/genética
[Mh] Termos MeSH secundário: Algoritmos
Animais
Proteínas de Drosophila/genética
Heterocromatina/metabolismo
Mutação
Proteínas do Grupo Polycomb/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Heterochromatin); 0 (Histones); 0 (Polycomb-Group Proteins)
[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:171202
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0163-z


  2 / 6030 MEDLINE  
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[PMID]:29208645
[Au] Autor:Mariezcurrena A; Uhlmann F
[Ad] Endereço:Chromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, United Kingdom.
[Ti] Título:Observation of DNA intertwining along authentic budding yeast chromosomes.
[So] Source:Genes Dev;31(21):2151-2161, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA replication of circular genomes generates physically interlinked or catenated sister DNAs. These are resolved through transient DNA fracture by type II topoisomerases to permit chromosome segregation during cell division. Topoisomerase II is similarly required for linear chromosome segregation, suggesting that linear chromosomes also remain intertwined following DNA replication. Indeed, chromosome resolution defects are a frequent cause of chromosome segregation failure and consequent aneuploidies. When and where intertwines arise and persist along linear chromosomes are not known, owing to the difficulty of demonstrating intertwining of linear DNAs. Here, we used excision of chromosomal regions as circular "loop outs" to convert sister chromatid intertwines into catenated circles. This revealed intertwining at replication termination and cohesin-binding sites, where intertwines are thought to arise and persist but not to a greater extent than elsewhere in the genome. Intertwining appears to spread evenly along chromosomes but is excluded from heterochromatin. We found that intertwines arise before replication termination, suggesting that replication forks rotate during replication elongation to dissipate torsion ahead of the forks. Our approach provides previously inaccessible insight into the topology of eukaryotic chromosomes and illuminates a process critical for successful chromosome segregation.
[Mh] Termos MeSH primário: Cromossomos Fúngicos/metabolismo
Replicação do DNA
DNA Fúngico/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Segregação de Cromossomos
Estruturas Genéticas
Genoma Fúngico
Heterocromatina/metabolismo
Origem de Replicação/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (DNA, Fungal); 0 (Heterochromatin); 0 (cohesins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1101/gad.305557.117


  3 / 6030 MEDLINE  
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[PMID]:28741530
[Au] Autor:Voon HPJ; Collas P; Wong LH
[Ad] Endereço:Department of Biochemistry and Molecular Biology, The Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.
[Ti] Título:Compromised Telomeric Heterochromatin Promotes ALTernative Lengthening of Telomeres.
[So] Source:Trends Cancer;2(3):114-116, 2016 Mar.
[Is] ISSN:2405-8025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alternative lengthening of telomeres (ALT) is an enigmatic process that allows certain cancers to maintain telomeres in the absence of telomerase. ALT cancers are frequently defective for ATRX/DAXX, a chaperone complex that deposits histone variant H3.3 at telomeres. We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX) prime ALT activation by disrupting telomeric heterochromatin.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Heterocromatina/metabolismo
Neoplasias/genética
Proteínas Nucleares/genética
Homeostase do Telômero
Proteína Nuclear Ligada ao X/genética
[Mh] Termos MeSH secundário: Seres Humanos
Mutação
Telômero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (DAXX protein, human); 0 (Heterochromatin); 0 (Nuclear Proteins); EC 3.6.4.12 (ATRX protein, human); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  4 / 6030 MEDLINE  
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[PMID]:28455402
[Au] Autor:Pinon V; Yao X; Dong A; Shen WH
[Ad] Endereço:Université de Strasbourg, Centre National de la Recherche Scientifique UPR2357, F-67000 Strasbourg, France (V.P., W.-H.S.).
[Ti] Título:SDG2-Mediated H3K4me3 Is Crucial for Chromatin Condensation and Mitotic Division during Male Gametogenesis in Arabidopsis.
[So] Source:Plant Physiol;174(2):1205-1215, 2017 Jun.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epigenetic reprogramming occurring during reproduction is crucial for both animal and plant development. Histone H3 Lys 4 trimethylation (H3K4me3) is an evolutionarily conserved epigenetic mark of transcriptional active euchromatin. While much has been learned in somatic cells, H3K4me3 deposition and function in gametophyte is poorly studied. Here, we demonstrate that SET DOMAIN GROUP2 (SDG2)-mediated H3K4me3 deposition participates in epigenetic reprogramming during Arabidopsis male gametogenesis. We show that loss of SDG2 barely affects meiosis and cell fate establishment of haploid cells. However, we found that SDG2 is critical for postmeiotic microspore development. Mitotic cell division progression is partly impaired in the loss-of-function mutant, particularly at the second mitosis setting up the two sperm cells. We demonstrate that SDG2 is involved in promoting chromatin decondensation in the pollen vegetative nucleus, likely through its role in H3K4me3 deposition, which prevents ectopic heterochromatic H3K9me2 speckle formation. Moreover, we found that derepression of the LTR retrotransposon is compromised in the vegetative cell of the mutant pollen. Consistent with chromatin condensation and compromised transcription activity, pollen germination and pollen tube elongation, representing the key function of the vegetative cell in transporting sperm cells during fertilization, are inhibited in the mutant. Taken together, we conclude that SDG2-mediated H3K4me3 is an essential epigenetic mark of the gametophyte chromatin landscape, playing critical roles in gamete mitotic cell cycle progression and pollen vegetative cell function during male gametogenesis and beyond.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/citologia
Arabidopsis/metabolismo
Cromatina/metabolismo
Gametogênese Vegetal
Histonas/metabolismo
Lisina/metabolismo
Mitose
[Mh] Termos MeSH secundário: Arabidopsis/genética
Núcleo Celular/metabolismo
Gametogênese Vegetal/genética
Regulação da Expressão Gênica de Plantas
Germinação/genética
Heterocromatina/metabolismo
Meiose/genética
Metilação
Mitose/genética
Mutação/genética
Pólen/crescimento & desenvolvimento
Pólen/metabolismo
Tubo Polínico/genética
Tubo Polínico/crescimento & desenvolvimento
Retroelementos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chromatin); 0 (Heterochromatin); 0 (Histones); 0 (Retroelements); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1104/pp.17.00306


  5 / 6030 MEDLINE  
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[PMID]:27779094
[Au] Autor:Böhmdorfer G; Sethuraman S; Rowley MJ; Krzyszton M; Rothi MH; Bouzit L; Wierzbicki AT
[Ad] Endereço:Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, United States.
[Ti] Título:Long non-coding RNA produced by RNA polymerase V determines boundaries of heterochromatin.
[So] Source:Elife;5, 2016 10 25.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA-mediated transcriptional gene silencing is a conserved process where small RNAs target transposons and other sequences for repression by establishing chromatin modifications. A central element of this process are long non-coding RNAs (lncRNA), which in are produced by a specialized RNA polymerase known as Pol V. Here we show that non-coding transcription by Pol V is controlled by preexisting chromatin modifications located within the transcribed regions. Most Pol V transcripts are associated with AGO4 but are not sliced by AGO4. Pol V-dependent DNA methylation is established on both strands of DNA and is tightly restricted to Pol V-transcribed regions. This indicates that chromatin modifications are established in close proximity to Pol V. Finally, Pol V transcription is preferentially enriched on edges of silenced transposable elements, where Pol V transcribes into TEs. We propose that Pol V may play an important role in the determination of heterochromatin boundaries.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Arabidopsis/genética
RNA Polimerases Dirigidas por DNA/metabolismo
Heterocromatina/metabolismo
RNA Longo não Codificante/metabolismo
RNA de Plantas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Argonauta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AGO4 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Argonaute Proteins); 0 (Heterochromatin); 0 (RNA, Long Noncoding); 0 (RNA, Plant); EC 2.7.7.- (RNA polymerase V, Arabidopsis); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171224
[Lr] Data última revisão:
171224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  6 / 6030 MEDLINE  
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[PMID]:27771437
[Au] Autor:Carranza PG; Gargantini PR; Prucca CG; Torri A; Saura A; Svärd S; Lujan HD
[Ad] Endereço:Laboratorio de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Católica de Córdoba, Argentina.
[Ti] Título:Specific histone modifications play critical roles in the control of encystation and antigenic variation in the early-branching eukaryote Giardia lamblia.
[So] Source:Int J Biochem Cell Biol;81(Pt A):32-43, 2016 12.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:During evolution, parasitic microorganisms have faced the challenges of adapting to different environments to colonize a variety of hosts. Giardia lamblia, a common cause of intestinal disease, has developed fascinating strategies to adapt both outside and inside its host's intestine, such as trophozoite differentiation into cyst and the switching of its major surface antigens. How gene expression is regulated during these adaptive processes remains undefined. Giardia lacks some typical eukaryotic features, like canonical transcription factors, linker histone H1, and complex promoter regions; suggesting that post-transcriptional and translational control of gene expression is essential for parasite survival. However, epigenetic factors may also play critical roles at the transcriptional level. Here, we describe the most common post-translational histone modifications; characterize enzymes involved in these reactions, and analyze their association with the Giardia's differentiation processes. We present evidence that NAD -dependent and NAD -independent histone deacetylases regulate encystation; however, a unique NAD -independent histone deacetylase modulate antigenic switching. The rates of acetylation of H4K8 and H4K16 are critical for encystation, whereas a decrease in acetylation of H4K8 and methylation of H3K9 occur preferentially during antigenic variation. These results show the complexity of the mechanisms regulating gene expression in this minimalistic protozoan parasite.
[Mh] Termos MeSH primário: Variação Antigênica
Giardia lamblia/imunologia
Giardia lamblia/metabolismo
Histonas/metabolismo
[Mh] Termos MeSH secundário: Acetilação/efeitos dos fármacos
Variação Antigênica/efeitos dos fármacos
Eucromatina/metabolismo
Giardia lamblia/citologia
Giardia lamblia/genética
Heterocromatina/metabolismo
Inibidores de Histona Desacetilases/farmacologia
Histona Desacetilases/metabolismo
Histonas/química
Lisina/metabolismo
NAD/metabolismo
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Euchromatin); 0 (Heterochromatin); 0 (Histone Deacetylase Inhibitors); 0 (Histones); 0U46U6E8UK (NAD); EC 3.5.1.98 (Histone Deacetylases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171217
[Lr] Data última revisão:
171217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE


  7 / 6030 MEDLINE  
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[PMID]:28449087
[Au] Autor:Zhang P; Rausch C; Hastert FD; Boneva B; Filatova A; Patil SJ; Nuber UA; Gao Y; Zhao X; Cardoso MC
[Ad] Endereço:Cell Biology and Epigenetics, Department of Biology, Technische Universität Darmstadt, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.
[Ti] Título:Methyl-CpG binding domain protein 1 regulates localization and activity of Tet1 in a CXXC3 domain-dependent manner.
[So] Source:Nucleic Acids Res;45(12):7118-7136, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytosine modifications diversify and structure the genome thereby controlling proper development and differentiation. Here, we focus on the interplay of the 5-methylcytosine reader Mbd1 and modifier Tet1 by analyzing their dynamic subcellular localization and the formation of the Tet oxidation product 5-hydroxymethylcytosine in mammalian cells. Our results demonstrate that Mbd1 enhances Tet1-mediated 5-methylcytosine oxidation. We show that this is due to enhancing the localization of Tet1, but not of Tet2 and Tet3 at heterochromatic DNA. We find that the recruitment of Tet1 and concomitantly its catalytic activity eventually leads to the displacement of Mbd1 from methylated DNA. Finally, we demonstrate that increased Tet1 heterochromatin localization and 5-methylcytosine oxidation are dependent on the CXXC3 domain of Mbd1, which recognizes unmethylated CpG dinucleotides. The Mbd1 CXXC3 domain deletion isoform, which retains only binding to methylated CpGs, on the other hand, blocks Tet1-mediated 5-methylcytosine to 5-hydroxymethylcytosine conversion, indicating opposite biological effects of Mbd1 isoforms. Our study provides new insights on how cytosine modifications, their modifiers and readers cross-regulate themselves.
[Mh] Termos MeSH primário: Ilhas de CpG
Proteínas de Ligação a DNA/genética
DNA/metabolismo
Regulação da Expressão Gênica
Heterocromatina/metabolismo
Oxigenases de Função Mista/genética
Proteínas Proto-Oncogênicas/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: 5-Metilcitosina/análogos & derivados
5-Metilcitosina/metabolismo
Animais
Linhagem Celular
DNA/genética
Proteínas de Ligação a DNA/metabolismo
Dioxigenases/genética
Dioxigenases/metabolismo
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HEK293
Heterocromatina/química
Seres Humanos
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Camundongos
Oxigenases de Função Mista/metabolismo
Células-Tronco Embrionárias Murinas/citologia
Células-Tronco Embrionárias Murinas/metabolismo
Mioblastos/citologia
Mioblastos/metabolismo
Oxirredução
Domínios Proteicos
Proteínas Proto-Oncogênicas/metabolismo
Transdução de Sinais
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Heterochromatin); 0 (Luminescent Proteins); 0 (MBD1 protein, human); 0 (Proto-Oncogene Proteins); 0 (TET2 protein, human); 0 (Transcription Factors); 0 (enhanced green fluorescent protein); 0 (red fluorescent protein); 1123-95-1 (5-hydroxymethylcytosine); 147336-22-9 (Green Fluorescent Proteins); 6R795CQT4H (5-Methylcytosine); 9007-49-2 (DNA); EC 1.- (Mixed Function Oxygenases); EC 1.- (TET1 protein, human); EC 1.- (TET3 protein, human); EC 1.13.11.- (Dioxygenases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx281


  8 / 6030 MEDLINE  
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[PMID]:28743002
[Au] Autor:Colmenares SU; Swenson JM; Langley SA; Kennedy C; Costes SV; Karpen GH
[Ad] Endereço:Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: sucolmenares@lbl.gov.
[Ti] Título:Drosophila Histone Demethylase KDM4A Has Enzymatic and Non-enzymatic Roles in Controlling Heterochromatin Integrity.
[So] Source:Dev Cell;42(2):156-169.e5, 2017 07 24.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic genomes are broadly divided between gene-rich euchromatin and the highly repetitive heterochromatin domain, which is enriched for proteins critical for genome stability and transcriptional silencing. This study shows that Drosophila KDM4A (dKDM4A), previously characterized as a euchromatic histone H3 K36 demethylase and transcriptional regulator, predominantly localizes to heterochromatin and regulates heterochromatin position-effect variegation (PEV), organization of repetitive DNAs, and DNA repair. We demonstrate that dKDM4A demethylase activity is dispensable for PEV. In contrast, dKDM4A enzymatic activity is required to relocate heterochromatic double-strand breaks outside the domain, as well as for organismal survival when DNA repair is compromised. Finally, DNA damage triggers dKDM4A-dependent changes in the levels of H3K56me3, suggesting that dKDM4A demethylates this heterochromatic mark to facilitate repair. We conclude that dKDM4A, in addition to its previously characterized role in euchromatin, utilizes both enzymatic and structural mechanisms to regulate heterochromatin organization and functions.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/enzimologia
Heterocromatina/metabolismo
Histona Desmetilases/metabolismo
[Mh] Termos MeSH secundário: Animais
Biocatálise
Ciclo Celular/genética
Pontos de Checagem do Ciclo Celular/genética
Efeitos da Posição Cromossômica/genética
Quebras de DNA de Cadeia Dupla
Reparo do DNA/genética
Proteínas de Drosophila/química
Drosophila melanogaster/genética
Fertilidade/genética
Regulação da Expressão Gênica
Inativação Gênica
Histonas/metabolismo
Lisina/metabolismo
Metilação
Mutação/genética
Domínios Proteicos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Heterochromatin); 0 (Histones); EC 1.14.11.- (Histone Demethylases); EC 1.5.- (KDM4A protein, Drosophila); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  9 / 6030 MEDLINE  
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[PMID]:29069084
[Au] Autor:Dahal BK; Kadyrova LY; Delfino KR; Rogozin IB; Gujar V; Lobachev KS; Kadyrov FA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL, United States of America.
[Ti] Título:Involvement of DNA mismatch repair in the maintenance of heterochromatic DNA stability in Saccharomyces cerevisiae.
[So] Source:PLoS Genet;13(10):e1007074, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heterochromatin contains a significant part of nuclear DNA. Little is known about the mechanisms that govern heterochromatic DNA stability. We show here that in the yeast Saccharomyces cerevisiae (i) DNA mismatch repair (MMR) is required for the maintenance of heterochromatic DNA stability, (ii) MutLα (Mlh1-Pms1 heterodimer), MutSα (Msh2-Msh6 heterodimer), MutSß (Msh2-Msh3 heterodimer), and Exo1 are involved in MMR at heterochromatin, (iii) Exo1-independent MMR at heterochromatin frequently leads to the formation of Pol ζ-dependent mutations, (iv) MMR cooperates with the proofreading activity of Pol ε and the histone acetyltransferase Rtt109 in the maintenance of heterochromatic DNA stability, (v) repair of base-base mismatches at heterochromatin is less efficient than repair of base-base mismatches at euchromatin, and (vi) the efficiency of repair of 1-nt insertion/deletion loops at heterochromatin is similar to the efficiency of repair of 1-nt insertion/deletion loops at euchromatin.
[Mh] Termos MeSH primário: Reparo de Erro de Pareamento de DNA
DNA Fúngico/química
Heterocromatina
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Dano ao DNA
DNA Fúngico/genética
Exodesoxirribonucleases/genética
Genes pol
Histona Acetiltransferases/genética
Proteínas MutL/genética
Proteína MutS de Ligação de DNA com Erro de Pareamento/genética
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Heterochromatin); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Rtt109 protein, S cerevisiae); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.1 (exodeoxyribonuclease I); EC 3.6.1.3 (MutL Proteins); EC 3.6.1.3 (MutS DNA Mismatch-Binding Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171026
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007074


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[PMID]:29030538
[Au] Autor:Bartholomew B
[Ad] Endereço:From the Department of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Houston, Texas 77030 bbartholomew@mdanderson.org.
[Ti] Título:Proteasomes beyond proteolysis: Roles in heterochromatin maintenance.
[So] Source:J Biol Chem;292(41):17156-17157, 2017 10 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In addition to its proteolytic roles, the 26S proteasome is involved in regulating transcription and in promoting sites of active chromatin. In this report, Seo provide evidence that the non-proteolytic 19S subunit of the 26S proteasome also regulates the spreading of inactive chromatin referred to as heterochromatin, suggesting further non-canonical roles of the proteasome in gene expression.
[Mh] Termos MeSH primário: Complexo de Endopeptidases do Proteassoma/genética
Proteólise
[Mh] Termos MeSH secundário: Citoplasma
Heterocromatina
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Heterochromatin); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171015
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.790824



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