Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
about
Sumoylation and transcription regulation at nuclear poresRedundant mechanisms are used by Ssn6-Tup1 in repressing chromosomal gene transcription in Saccharomyces cerevisiae.Histone deacetylases RPD3 and HOS2 regulate the transcriptional activation of DNA damage-inducible genes.Identification of novel activation mechanisms for FLO11 regulation in Saccharomyces cerevisiaeSsn6-Tup1 requires the ISW2 complex to position nucleosomes in Saccharomyces cerevisiae.Molecular genetic analysis of the yeast repressor Rfx1/Crt1 reveals a novel two-step regulatory mechanism.The Tup1 corepressor directs Htz1 deposition at a specific promoter nucleosome marking the GAL1 gene for rapid activation.Multiple histone deacetylases are recruited by corepressor Sin3 and contribute to gene repression mediated by Opi1 regulator of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae.Activator Gcn4p and Cyc8p/Tup1p are interdependent for promoter occupancy at ARG1 in vivoStochastic and regulatory role of chromatin silencing in genomic response to environmental changesHOS2 and HDA1 encode histone deacetylases with opposing roles in Candida albicans morphogenesis.The LAMMER kinase homolog, Lkh1, regulates Tup transcriptional repressors through phosphorylation in Schizosaccharomyces pombe.Sum1p, the origin recognition complex, and the spreading of a promoter-specific repressor in Saccharomyces cerevisiae.The general transcriptional repressor Tup1 is required for dimorphism and virulence in a fungal plant pathogenHairless is a cofactor for Runt-dependent transcriptional regulationTup1 stabilizes promoter nucleosome positioning and occupancy at transcriptionally plastic genes.The Cyc8-Tup1 complex inhibits transcription primarily by masking the activation domain of the recruiting protein.Chromatin and transcription in yeastThe Hos2 Histone Deacetylase Controls Ustilago maydis Virulence through Direct Regulation of Mating-Type GenesThe histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cellsFunction and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiaeHigh-sensitivity TFA-free LC-MS for profiling histonesLife within a community: benefit to yeast long-term survival.Transcriptional repression by Tup1-Ssn6.Stabilization of the promoter nucleosomes in nucleosome-free regions by the yeast Cyc8-Tup1 corepressor.A fungal family of transcriptional regulators: the zinc cluster proteinsQuantitative dynamics of the link between cellular metabolism and histone acetylation.Mth1 regulates the interaction between the Rgt1 repressor and the Ssn6-Tup1 corepressor complex by modulating PKA-dependent phosphorylation of Rgt1.Enhancing drug accumulation in Saccharomyces cerevisiae by repression of pleiotropic drug resistance genes with chimeric transcription repressors.The glucose signaling network in yeastLiquid chromatography mass spectrometry profiling of histonesTranscriptional repression of target genes by LEUNIG and SEUSS, two interacting regulatory proteins for Arabidopsis flower development.The Saccharomyces cerevisiae TRT2 tRNAThr gene upstream of STE6 is a barrier to repression in MATalpha cells and exerts a potential tRNA position effect in MATa cells.Specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation and retrotransposon silencing.A chromatin-mediated mechanism for specification of conditional transcription factor targets.Functional comparison of the Tup11 and Tup12 transcriptional corepressors in fission yeast.An Smc3 acetylation cycle is essential for establishment of sister chromatid cohesion.Choose Your Own Adventure: The Role of Histone Modifications in Yeast Cell Fate.Shields up: the Tup1-Cyc8 repressor complex blocks coactivator recruitmentEffect of sequence-directed nucleosome disruption on cell-type-specific repression by alpha2/Mcm1 in the yeast genome.
P2860
Q26999229-428C5E6E-3830-4CBD-BF7A-1236461DFBECQ27930073-DAB111AD-3C95-4FBC-AF2E-05548F98F8FEQ27932545-C6E8CDDB-63A3-4B81-9C03-B2E08F2F9608Q27934533-025FFAF2-9476-441E-B243-4E6D3C3FA753Q27936035-8E4109B9-C34A-4726-88B3-9AA71F8E205FQ27936066-EAC3AB4E-8F48-4F0F-BC8D-3C5516807B55Q27936207-7754D7BA-B8CC-482F-809A-D49010FFC8EDQ27940286-BD68FFDA-4F59-42AD-900B-B82716B57AC4Q33228027-2DBFC227-8101-4293-8CA8-6E67FAF4E653Q33361585-0B968F7E-CFEA-4920-AE68-9F17DADAEED1Q33668741-EC1FD195-8F97-4E4D-BA69-B703DC6EE090Q33810112-5F11F65F-A16C-4D1B-B7EF-69BD4C2E50E9Q33884148-C685C629-8163-43CD-B59F-1EABE5934F1BQ34016251-F26C30E2-64D8-431A-A680-6C8678F049AEQ34803072-EF021A48-11ED-44A0-8705-3C59A7D67B88Q35468491-8506AE60-F97B-414E-AB81-9D55F1944A48Q35624743-89074E2C-C683-47D6-A120-2EF467AA3268Q35748234-A67ABEA6-2A45-4DF7-BD4A-7B272011DA9FQ35758627-047220F4-B80B-45CA-BAA1-EEACF388AEA0Q35861844-F3AD158C-6B13-43E7-B4DB-EE49B873C362Q36076499-EA046A14-B777-4576-AC57-4CA86017D039Q36453034-2D245A21-8348-42DA-B272-55F2A3423363Q36566606-561D43FD-88B5-406A-AC49-291E0075BB73Q36579338-8CE159C2-B6DD-4F54-9CAB-E6817AE2EE7AQ36580589-909CC5EE-CB37-4052-9DE4-F382C6E2A615Q36588772-6F388690-21BC-4723-9712-C0E32464EFA8Q36796895-78563AE0-FF45-4ABD-A222-C378B0171201Q36803220-58F4977B-8339-4D93-B54F-891DBCAC6D23Q37002693-7C8A3078-F3EB-4ADF-9D34-FA3C7E56DDC2Q37202919-95BC8C8E-787A-470A-A409-DD2E03139114Q37222851-63A37185-1A33-4244-9623-CB1F87028381Q37388945-8106F77D-E8BC-495D-8702-6CBE30A1EB59Q37564284-838B7C84-724D-408F-8D29-D0D8325708ADQ38302551-03E14E2A-3528-40E0-89E9-C0BDEE3E3103Q38307684-A8C28F09-83E7-4F20-88AE-9F1EB7BF31C0Q38332463-751D7C19-BF9A-429A-9D83-B10B6958B67DQ38625008-49D33AFC-4E12-4EA2-B0D0-2DC05A2AF0D7Q38987852-530305BB-D928-4260-8A21-B956C12B49F4Q39923594-72392D12-64C1-4C7C-9F58-F355402B03A7Q40929079-4A0FD4D7-140C-449A-A029-702EF684CE9C
P2860
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@ast
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@en
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@nl
type
label
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@ast
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@en
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@nl
prefLabel
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@ast
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@en
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.
@nl
P2093
P2860
P356
P1476
Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo
@en
P2093
Cherie B Coco
Diane G Edmondson
Judith K Davie
P2860
P304
50158-50162
P356
10.1074/JBC.M309753200
P407
P50
P577
2003-10-02T00:00:00Z