Source:http://linkedlifedata.com/resource/pubmed/id/11029700
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2000-11-13
|
| pubmed:abstractText |
cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremula X tremuloides) and rice (Oryza sativa) plants, and were designated Pt;cycH;1 and Os;cycH;1, respectively. The deduced amino-acid sequences showed 40-60% similarity to human cyclin H and Schizosaccharomyces pombe Mcs2, with higher similarity in the cyclin box region. While Pt;cycH;1 and Os;cycH;1 were expressed in all tissues examined, the transcripts accumulated abundantly in dividing cells. Expression of Os;cycH;1 was abundant in the S-phase in partially synchronized suspension cells, and was induced by submergence in internodes of deepwater rice. A yeast two-hybrid assay demonstrated that both Pt;CycH;1 and Os;CycH;1 were able to interact with rice R2 kinase, which is structurally and functionally similar to cyclin-dependent kinase (CDK)-activating kinase (CAK) of vertebrates. Moreover, an in vitro pull-down assay showed that Os;CycH;1 specifically bound to R2 but not to other rice CDKs. When R2 was expressed in budding yeast CAK mutant, the suppression activity in terms of temperature-sensitivity was enhanced by co-expression with Os;cycH;1. Furthermore, in vitro kinase assay indicated that the kinase activities of R2 on CDKs and the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II were markedly elevated by binding to Os;CycH;1. Our results suggest that cyclin H is a regulatory subunit of CAK, which positively controls CDK- and CTD-kinase activities in plant cells.
|
| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/CDK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cyclin-dependent kinase-activating...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0960-7412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
24
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
11-20
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:11029700-Amino Acid Sequence,
pubmed-meshheading:11029700-Animals,
pubmed-meshheading:11029700-CDC2-CDC28 Kinases,
pubmed-meshheading:11029700-Cell Cycle,
pubmed-meshheading:11029700-Cloning, Molecular,
pubmed-meshheading:11029700-Cyclin-Dependent Kinase 2,
pubmed-meshheading:11029700-Cyclin-Dependent Kinases,
pubmed-meshheading:11029700-Cyclins,
pubmed-meshheading:11029700-Enzyme Activation,
pubmed-meshheading:11029700-Humans,
pubmed-meshheading:11029700-Molecular Sequence Data,
pubmed-meshheading:11029700-Oryza sativa,
pubmed-meshheading:11029700-Phylogeny,
pubmed-meshheading:11029700-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11029700-Recombinant Proteins,
pubmed-meshheading:11029700-Saccharomyces cerevisiae,
pubmed-meshheading:11029700-Sequence Alignment,
pubmed-meshheading:11029700-Sequence Homology, Amino Acid,
pubmed-meshheading:11029700-Trees
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.
|
| pubmed:affiliation |
Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|