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Cdc28 kinase activity regulates the basal transcription machinery at a subset of genes
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
22689984
retrieved
1 December 2016
title
Cdc28 kinase activity regulates the basal transcription machinery at a subset of genes
(English)
1 reference
stated in
PubMed
PubMed ID
22689984
retrieved
1 December 2016
main subject
Cyclin-dependent serine/threonine-protein kinase CDC28 YBR160W
1 reference
stated in
GOA release 2020-03-11
TFIIH complex serine/threonine-protein kinase subunit KIN28 YDL108W
1 reference
stated in
GOA release 2020-03-11
author
Magnar Bjørås
series ordinal
6
object named as
Magnar Bjørås
0 references
Pierre Chymkowitch
object named as
Pierre Chymkowitch
series ordinal
1
0 references
Vegard Eldholm
object named as
Vegard Eldholm
series ordinal
2
0 references
Jessica M Lindvall
object named as
Jessica M Lindvall
series ordinal
5
0 references
author name string
Susanne Lorenz
series ordinal
3
0 references
Christine Zimmermann
series ordinal
4
0 references
Leonardo A Meza-Zepeda
series ordinal
7
0 references
Jorrit M Enserink
series ordinal
8
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language of work or name
English
0 references
publication date
26 June 2012
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published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
22689984
retrieved
1 December 2016
volume
109
0 references
page(s)
10450-5
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issue
26
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cites work
The multifunctional Ccr4-Not complex directly promotes transcription elongation
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Cks1, Cdk1, and the 19S proteasome collaborate to regulate gene induction-dependent nucleosome eviction in yeast
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TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II.
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Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation
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Histone H2B ubiquitylation is associated with elongating RNA polymerase II
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A kinase-independent function of Cks1 and Cdk1 in regulation of transcription
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Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
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The Paf1 complex physically and functionally associates with transcription elongation factors in vivo
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Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.
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Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II.
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Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
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Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
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A chemical-genetic screen to unravel the genetic network of CDC28/CDK1 links ubiquitin and Rad6-Bre1 to cell cycle progression
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The phosphorylation of the androgen receptor by TFIIH directs the ubiquitin/proteasome process
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ChIP-Seq using high-throughput DNA sequencing for genome-wide identification of transcription factor binding sites
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29 September 2017
TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II
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Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7.
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Serine-7 of the RNA polymerase II CTD is specifically required for snRNA gene expression
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Chemical inhibition of the TFIIH-associated kinase Cdk7/Kin28 does not impair global mRNA synthesis.
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C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats
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Isolation and characterization of rabbit anti-m3 2,2,7G antibodies
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29 September 2017
Identification of phosphorylation sites in the repetitive carboxyl-terminal domain of the mouse RNA polymerase II largest subunit.
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2 June 2018
Cks1-dependent proteasome recruitment and activation of CDC20 transcription in budding yeast
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Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2
1 reference
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Crossref
reference URL
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retrieved
21 January 2018
Identifiers
DOI
10.1073/PNAS.1200067109
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ADS bibcode
2012PNAS..10910450C
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PMCID
3387082
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PubMed ID
22689984
1 reference
stated in
PubMed
PubMed ID
22689984
retrieved
1 December 2016
ResearchGate publication ID
225293786
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