Linked Life Data

8521393

Source:http://linkedlifedata.com/resource/pubmed/id/8521393

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1996-1-22
pubmed:databankReference
pubmed:abstractText
Mammalian CDK7 is a protein kinase identified as the catalytic subunit of cyclin-dependent kinase (CDK)-activating kinase and as an essential component of the transcription factor TFIIH that is involved in transcription initiation and DNA repair. We have identified in human cells a number of CDK7-associated cellular proteins that appear to fall into two classes based on their relative [35S] metabolic labeling intensity. One class of proteins present in CDK7 immunocomplexes as a minor fraction contains components of the TFIIH transcription complex such as p62 and p89ERCC3, whereas the other fraction contains four polypeptides (p35, p37Cyclin H, p75, and p95) that are stoichiometrically associated with CDK7. Whereas the levels of association of p35, p37Cyclin H, and p75 with CDK7 remain unchanged between density-arrested and proliferating Ewing sarcoma EW-1 cells, the association of p95 with CDK7 was significantly decreased as cells reached confluency. Through a large-scale immunopurification of CDK7 complexes and protein microsequencing, we have isolated a cDNA that encodes p35 and have shown that it is the human homologue of Mat1 that is involved in the assembly of CAK. MAT1 contains a highly conserved C3HC4 motif at its NH2 terminus, a characteristic feature shared among RING finger proteins. The human MAT1 gene expresses a single 1.6-kb transcript, the steady-state level of which, like CDK7 and cyclin H, varies significantly in different cell lines and in different terminally differentiated tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6058-62
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8521393-Amino Acid Sequence, pubmed-meshheading:8521393-Base Sequence, pubmed-meshheading:8521393-Cell Cycle, pubmed-meshheading:8521393-Cloning, Molecular, pubmed-meshheading:8521393-Cyclin H, pubmed-meshheading:8521393-Cyclin-Dependent Kinases, pubmed-meshheading:8521393-Cyclins, pubmed-meshheading:8521393-Gene Expression, pubmed-meshheading:8521393-HeLa Cells, pubmed-meshheading:8521393-Humans, pubmed-meshheading:8521393-Macromolecular Substances, pubmed-meshheading:8521393-Molecular Sequence Data, pubmed-meshheading:8521393-Molecular Weight, pubmed-meshheading:8521393-Neoplasm Proteins, pubmed-meshheading:8521393-Protein-Serine-Threonine Kinases, pubmed-meshheading:8521393-RNA, Messenger, pubmed-meshheading:8521393-Sequence Alignment, pubmed-meshheading:8521393-Sequence Homology, Amino Acid
pubmed:year
1995
pubmed:articleTitle
Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill 27599-3280, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.