A motif shared by TFIIF and TFIIB mediates their interaction with the RNA polymerase II carboxy-terminal domain phosphatase Fcp1p in Saccharomyces cerevisiae
about
A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNPMolecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIFThe C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylationNMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1Conceptual Model-based Systems Biology: mapping knowledge and discovering gaps in the mRNA transcription cycleCrystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIFThe transcriptional coactivator PC4/Sub1 has multiple functions in RNA polymerase II transcription.Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry.Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunitsAmino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II.TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcriptionIdentification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylationOpposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domainRNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and TemplateSchizosaccharomyces pombe carboxyl-terminal domain (CTD) phosphatase Fcp1: distributive mechanism, minimal CTD substrate, and active site mapping.Formation of a carboxy-terminal domain phosphatase (Fcp1)/TFIIF/RNA polymerase II (pol II) complex in Schizosaccharomyces pombe involves direct interaction between Fcp1 and the Rpb4 subunit of pol IIThe TFIIB tip domain couples transcription initiation to events involved in RNA processingCell cycle regulators interact with pathways that modulate microtubule stability in Saccharomyces cerevisiae.Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.Dephosphorylating eukaryotic RNA polymerase IICross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Structural and binding studies of the C-terminal domains of yeast TFIIF subunits Tfg1 and Tfg2.Transcription activation by targeted recruitment of the RNA polymerase II CTD phosphatase FCP1.AtCPL5, a novel Ser-2-specific RNA polymerase II C-terminal domain phosphatase, positively regulates ABA and drought responses in Arabidopsis.Sub1/PC4, a multifaceted factor: from transcription to genome stability.Cellular splicing and transcription regulatory protein p32 represses adenovirus major late transcription and causes hyperphosphorylation of RNA polymerase II.Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly.Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity.Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1.Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator.Identification of Novel Biomarkers for Behcet Disease Diagnosis Using Human Proteome Microarray Approach.Structural dissection of an interaction between transcription initiation and termination factors implicated in promoter-terminator cross-talk.
P2860
Q24300798-942837CF-8CC1-4E3C-873D-D17F7E20BB32Q24540277-7C4CCB05-8AE9-4E1E-857C-395C888437D9Q24550508-12C3E812-0942-48E8-863C-6389384EE2F8Q24553649-2F5E4907-DC25-487E-BCEC-B7B8C9DA9672Q24553772-FCEEA293-338B-4B5D-A5C5-07794885A28CQ24675208-ACA585C3-11DD-4D07-9BE7-52C9CD932FA0Q27331366-45ABBBEF-B007-4C09-B8AB-ED45E0E084C0Q27630607-1991D284-2A28-4EFE-8344-9F17345302A2Q27930005-5B8B3799-0EAC-4BE9-B551-FCACB2341DC3Q27930175-F64CD9A2-8B1F-4CA9-8480-B62D6D09BAA3Q27933967-B99E5E78-4801-4CBE-AFCE-355DE89EAE1DQ27934170-EB7319F8-6D5A-4C49-A33D-F83F8F69B88FQ27939300-8CBBBE82-3F89-4F72-9348-DD9428804EC2Q28188877-067D67D5-5B7C-4888-85EE-309BCFDBB407Q28304227-CAD8B217-7DE9-40E0-BA4D-6BB52FA3D474Q28343959-0BB1D28A-B7C5-4B62-8102-140D0268E99FQ29540749-44A36B7E-FB18-48E6-A344-5478886AED4DQ33196328-501283E3-E0F7-4131-A679-D0A8B414C272Q34302645-58367088-F001-4FA9-A732-88953B114C8CQ34400749-BC78F712-10BF-4E36-B06A-A9580DA1E40EQ35598286-E7F5DB14-5D76-4598-BC54-F60018945DF4Q35621442-F37D43AD-B905-4745-8892-2607FFF9CF99Q36600950-9BBCB742-5590-41F4-815F-F17FEBA726DEQ38182821-2F412301-4D2F-43D5-9EB5-69F6BCD59320Q38330176-FE90EDCF-B0E9-412D-93ED-7F84F0CDA4D9Q39097740-84A14A3D-B521-4EA6-BAFE-AE4600674144Q39107561-D52197A1-AF46-48CD-9A8C-B1EDECF5455DQ39342931-A5B65F21-788D-420A-A48A-9485638D2AA2Q40287167-0FC4B3E7-B160-41F1-8BE8-CB3F165B4FE9Q42709937-92EFB7E1-4CE7-4714-AFF4-C8EEA3B7D308Q43948899-FC4E4FE6-430A-450B-865F-871010840842Q44077335-27BF63A4-8CE3-4F85-9040-3B407C39E583Q44295702-05A86497-5896-4E8B-BA29-C93D5A4C74DAQ45162501-EDF273D1-54EF-4E09-8EC4-0A1923469751Q48958217-EBC17375-A17C-468B-9B5B-E0B29E6BB4E8Q50173461-6C088A21-6675-40D9-808B-61FC0E458D4A
P2860
A motif shared by TFIIF and TFIIB mediates their interaction with the RNA polymerase II carboxy-terminal domain phosphatase Fcp1p in Saccharomyces cerevisiae
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
name
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@ast
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@en
A motif shared by TFIIF and TF ...... p in Saccharomyces cerevisiae.
@nl
type
label
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@ast
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@en
A motif shared by TFIIF and TF ...... p in Saccharomyces cerevisiae.
@nl
prefLabel
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@ast
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@en
A motif shared by TFIIF and TF ...... p in Saccharomyces cerevisiae.
@nl
P2093
P2860
P1476
A motif shared by TFIIF and TF ...... 1p in Saccharomyces cerevisiae
@en
P2093
J Greenblatt
J Omichinski
P2860
P304
P356
10.1128/MCB.20.20.7438-7449.2000
P407
P577
2000-10-01T00:00:00Z