Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants. Yamaguchi, M., Fabian, T., Sauter, M., Bhalerao, R. P., Schrader, J., Sandberg, G., Umeda, M., & Uchimiya, H. The Plant Journal, 24(1):11–20, 2000. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-313x.2000.00846.x![Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremulax 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.
@article{yamaguchi_activation_2000,
title = {Activation of {CDK}-activating kinase is dependent on interaction with {H}-type cyclins in plants},
volume = {24},
issn = {1365-313X},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1046/j.1365-313x.2000.00846.x},
doi = {10/cxkrs9},
abstract = {cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremulax 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.},
language = {en},
number = {1},
urldate = {2021-11-08},
journal = {The Plant Journal},
author = {Yamaguchi, Masatoshi and Fabian, Tanja and Sauter, Margret and Bhalerao, Rishikesh P. and Schrader, Jarmo and Sandberg, Göran and Umeda, Masaaki and Uchimiya, Hirofumi},
year = {2000},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-313x.2000.00846.x},
keywords = {CDK-activating kinase, cell cycle, cyclin H, cyclin-dependent protein kinase, poplar, rice},
pages = {11--20},
}
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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.","language":"en","number":"1","urldate":"2021-11-08","journal":"The Plant Journal","author":[{"propositions":[],"lastnames":["Yamaguchi"],"firstnames":["Masatoshi"],"suffixes":[]},{"propositions":[],"lastnames":["Fabian"],"firstnames":["Tanja"],"suffixes":[]},{"propositions":[],"lastnames":["Sauter"],"firstnames":["Margret"],"suffixes":[]},{"propositions":[],"lastnames":["Bhalerao"],"firstnames":["Rishikesh","P."],"suffixes":[]},{"propositions":[],"lastnames":["Schrader"],"firstnames":["Jarmo"],"suffixes":[]},{"propositions":[],"lastnames":["Sandberg"],"firstnames":["Göran"],"suffixes":[]},{"propositions":[],"lastnames":["Umeda"],"firstnames":["Masaaki"],"suffixes":[]},{"propositions":[],"lastnames":["Uchimiya"],"firstnames":["Hirofumi"],"suffixes":[]}],"year":"2000","note":"_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-313x.2000.00846.x","keywords":"CDK-activating kinase, cell cycle, cyclin H, cyclin-dependent protein kinase, poplar, rice","pages":"11–20","bibtex":"@article{yamaguchi_activation_2000,\n\ttitle = {Activation of {CDK}-activating kinase is dependent on interaction with {H}-type cyclins in plants},\n\tvolume = {24},\n\tissn = {1365-313X},\n\turl = {https://onlinelibrary.wiley.com/doi/abs/10.1046/j.1365-313x.2000.00846.x},\n\tdoi = {10/cxkrs9},\n\tabstract = {cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremulax tremuloides) and rice (Oryza sativa) plants, and were designated Pt;cycH;1 and Os;cycH;1, respectively. 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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.},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2021-11-08},\n\tjournal = {The Plant Journal},\n\tauthor = {Yamaguchi, Masatoshi and Fabian, Tanja and Sauter, Margret and Bhalerao, Rishikesh P. and Schrader, Jarmo and Sandberg, Göran and Umeda, Masaaki and Uchimiya, Hirofumi},\n\tyear = {2000},\n\tnote = {\\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-313x.2000.00846.x},\n\tkeywords = {CDK-activating kinase, cell cycle, cyclin H, cyclin-dependent protein kinase, poplar, rice},\n\tpages = {11--20},\n}\n\n","author_short":["Yamaguchi, M.","Fabian, T.","Sauter, M.","Bhalerao, R. 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