pubmed-article:10958787 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10958787 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:10958787 | lifeskim:mentions | umls-concept:C1413288 | lld:lifeskim |
pubmed-article:10958787 | lifeskim:mentions | umls-concept:C1415545 | lld:lifeskim |
pubmed-article:10958787 | lifeskim:mentions | umls-concept:C0385592 | lld:lifeskim |
pubmed-article:10958787 | pubmed:issue | 45 | lld:pubmed |
pubmed-article:10958787 | pubmed:dateCreated | 2000-11-27 | lld:pubmed |
pubmed-article:10958787 | pubmed:abstractText | Cyclin-dependent kinase 7 (Cdk7) forms a trimeric complex with cyclin H and Mat1 to form the mammalian Cdk-activating kinase, CAK, as well as a part of the basal transcription factor TFIIH, where Cdk7 phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II. Here, we report a novel interaction between Cdk7 and a histidine triad (HIT) family protein, Hint/PKCI-1. This interaction was initially observed in a yeast two-hybrid study and subsequently verified by co-immunoprecipitation and subcellular localization studies, where overexpression of Cdk7 leads to partial relocalization of Hint to the nucleus. The physical association is independent of cyclin H binding or Cdk7 kinase activity and is conserved between the related Sacharomyces cerevisiae CTD kinase Kin28 and the HIT protein Hnt1. Furthermore, combination of a disruption of HNT1 and a KIN28 temperature-sensitive allele in S. cerevisiae led to highly elongated cell morphology and reduced colony formation, indicating a genetic interaction between KIN28 and HNT1. The physical and genetic interactions of Hint and Hnt1 with Cdk7 and Kin28 suggest a role for this class of histidine triad proteins in the regulation of Cdk7 and Kin28 functions. | lld:pubmed |
pubmed-article:10958787 | pubmed:language | eng | lld:pubmed |
pubmed-article:10958787 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10958787 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10958787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10958787 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10958787 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10958787 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10958787 | pubmed:author | pubmed-author:MäkeläT PTP | lld:pubmed |
pubmed-article:10958787 | pubmed:author | pubmed-author:KorsisaariNN | lld:pubmed |
pubmed-article:10958787 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10958787 | pubmed:day | 10 | lld:pubmed |
pubmed-article:10958787 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10958787 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10958787 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10958787 | pubmed:pagination | 34837-40 | lld:pubmed |
pubmed-article:10958787 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10958787 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10958787 | pubmed:articleTitle | Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins. | lld:pubmed |
pubmed-article:10958787 | pubmed:affiliation | Haartman Institute & Biocentrum Helsinki, P. O. Box 21, University of Helsinki, 00014 Helsinki, Finland. | lld:pubmed |
pubmed-article:10958787 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10958787 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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