Linked Life Data

8761664

Source:http://linkedlifedata.com/resource/pubmed/id/8761664

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-10-4
pubmed:abstractText
The Kin28 protein kinase interacts physically and genetically with cyclin Ccl1. Kin28 has been reported recently to be involved in the in vivo phosphorylation of the largest subunit of RNA polymerase II (Rpb1) in Saccharomyces cerevisiae. Now, we show that in a strain harboring a conditional ccl1-ts mutation, the C-terminal domain (CTD) of the Rpb1 subunit is under-phosphorylated at restrictive temperature. The transcription of a set of genes, chosen at random, is severely affected in a kin28-ts mutant shifted at restrictive temperature. Here, we report that the same set of genes requires a functional CCL1 gene product to be transcribed. These findings, added to previously published data, establishes that Kin28p is a cyclin-dependent kinase (CDK) with Ccl1p as a companion, both of them being necessary for general transcription and CTD phosphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0764-4469
pubmed:author
pubmed:issnType
Print
pubmed:volume
319
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Ccl1, a cyclin associated with protein kinase Kin28, controls the phosphorylation of RNA polymerase II largest subunit and mRNA transcription.
pubmed:affiliation
Section de recherche, Institut Curie, Orsay, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't