Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast.
about
Uncoupling transcription from covalent histone modification.Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNAAutoacetylation of the histone acetyltransferase Rtt109Chromatin regulation and genome maintenance by mammalian SIRT6Histone H4 lysine 16 acetylation regulates cellular lifespanThe controversial world of sirtuinsPost-translational modifications of histones that influence nucleosome dynamicsHistone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferasesSirtuin-dependent epigenetic regulation in the maintenance of genome integrityImpacts on Sirtuin Function and Bioavailability of the Dietary Bioactive Compound DihydrocoumarinStructural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin SilencingTwo surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencingHeterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNAThe glucanosyltransferase Gas1 functions in transcriptional silencing.Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109.DNA polymerase epsilon, acetylases and remodellers cooperate to form a specialized chromatin structure at a tRNA insulator.Histone deacetylase Rpd3 antagonizes Sir2-dependent silent chromatin propagationSaccharomyces cerevisiae linker histone Hho1p functionally interacts with core histone H4 and negatively regulates the establishment of transcriptionally silent chromatinCul8/Rtt101 forms a variety of protein complexes that regulate DNA damage response and transcriptional silencingHst3 and Hst4 histone deacetylases regulate replicative lifespan by preventing genome instability in Saccharomyces cerevisiae.The SUMO E3 ligase Siz2 exerts a locus-dependent effect on gene silencing in Saccharomyces cerevisiaeSpt10 and Spt21 are required for transcriptional silencing in Saccharomyces cerevisiae.The role of multiple marks in epigenetic silencing and the emergence of a stable bivalent chromatin stateElevated histone expression promotes life span extensionThe C-terminus of histone H2B is involved in chromatin compaction specifically at telomeres, independently of its monoubiquitylation at lysine 123Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genomeThe Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS)Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity.Dissecting nucleosome free regions by a segmental semi-Markov model.Histone acetyltransferase Rtt109 is required for Candida albicans pathogenesis.EBV-positive Hodgkin lymphoma is associated with suppression of p21cip1/waf1 and a worse prognosis.Histone chaperone Chz1p regulates H2B ubiquitination and subtelomeric anti-silencing.Regulation of white and opaque cell-type formation in Candida albicans by Rtt109 and Hst3SIRT1 is necessary for proficient telomere elongation and genomic stability of induced pluripotent stem cells.Reconstitution of heterochromatin-dependent transcriptional gene silencing.Functional dissection of SIRT6: identification of domains that regulate histone deacetylase activity and chromatin localizationPreparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes.Dynamic chromatin localization of Sirt6 shapes stress- and aging-related transcriptional networks.Epigenetics in Saccharomyces cerevisiae.
P2860
Q21144875-D1AFA74D-7882-4495-99E5-FA42ACECB29AQ24306661-A36B3625-B1AD-4653-B736-2C46F3D4EEC8Q24632973-62C9A8DF-4294-4F3E-BF05-975A91F7094BQ24634557-09F75426-30A4-4A65-B1B1-9A0EB9FCE5B5Q24657553-1B676C17-A086-4FB3-887D-8F5252D02F8CQ26829146-D9C24B20-BAEA-4D58-8063-2F63265CCB95Q26852536-EDCCF4A5-025F-43FD-9539-42258CE1AF99Q27003952-03756ADC-288A-49DC-9BD1-21B6150EEFB3Q27026871-858D3BBB-F59F-4694-A4FB-E5E5DF10D3D1Q27321607-093BC4D3-599C-4C51-BD11-F73E9CBCB878Q27658650-6B4831DB-EB38-4BD0-A984-0788A1634ED5Q27676464-BAA4E961-CA33-4162-88E1-0F80ECAAF33FQ27678023-8FDAFD3C-BF11-4906-9143-FDFC7A366BC5Q27930585-E27850C2-A4ED-4760-A899-E7B5A0ADF2F5Q27932154-05F1507B-217A-4A9A-B18C-ACBC85B7BDCDQ27932706-1873B0B8-87EE-470C-AE4F-0D41CB4F31FBQ27932909-FE80F94C-BA76-44FD-9B7B-FEAB3B4EE71DQ27934859-429C5AAE-20AC-4569-AB73-F93CC5B7F9C1Q27935062-00929C98-14DB-44B4-B47E-E6F6C4731E2FQ27936956-FDF7C0DF-AC4D-4508-B774-7C4CB2106D90Q27939937-91C2379E-7E60-4885-B6B9-A09261318B9CQ27940068-C44C2B6A-D42B-48D0-BD24-1CB6E3F019FDQ28534712-B4CCAC6D-0C40-4EE3-9D03-7873FCD4D225Q28660674-05F711E4-5D98-4963-A249-9A85AB8AC55CQ28742012-7E8E294B-63B1-4D9C-A29F-FB63002B6907Q28756588-EC2A8F7A-2C25-4D14-A6E9-5DBFF3D5FF90Q30276142-9051F489-CB41-4816-90DD-7C424FB9DA00Q30411607-7DB0B6CF-4C77-404A-95F5-BC5707968B43Q30497676-DA199707-5AF7-4836-B13F-326C967B4905Q33415485-33C93BAF-3849-4DF2-A2C9-780453FBBB51Q33667782-BB5DAFD3-55DC-40F1-8359-0964E7E0CA15Q33711558-64C421C8-6BEE-4316-9749-794EBC3C75EAQ33719338-8B2E0832-DE43-4A48-828B-EFE6D97F94A8Q33727077-969133CF-DE64-4299-9E95-568D99BEB1C9Q33730161-08C1FFD5-F048-4600-B444-D4C98D82C8B6Q33743928-7AE1CE15-9740-4727-BD44-686D5DC31B6CQ33759201-BE23FCCE-4B55-492E-BA9E-7000CDC8B79CQ33817639-94807E37-DE0A-4F22-95B0-2387A9468B2DQ33954474-1E39E247-9E80-4329-B673-714B179C8995Q34037400-2DDB66DD-D0B0-4EF5-812F-26F1B9846EB3
P2860
Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@ast
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@en
type
label
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@ast
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@en
prefLabel
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@ast
Sir2 deacetylates histone H3 l ...... ochromatin structure in yeast.
@en
P2093
P2860
P1433
P1476
Sir2 deacetylates histone H3 l ...... rochromatin structure in yeast
@en
P2093
Kangling Zhang
Michael Grunstein
Qiongyi Zhang
P2860
P304
P356
10.1016/J.MOLCEL.2007.07.021
P50
P577
2007-09-01T00:00:00Z