Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.
Identifieur interne : 004827 ( Main/Corpus ); précédent : 004826; suivant : 004828Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.
Auteurs : M. Yamaguchi ; T. Fabian ; M. Sauter ; R P Bhalerao ; J. Schrader ; G. Sandberg ; M. Umeda ; H. UchimiyaSource :
- The Plant journal : for cell and molecular biology [ 0960-7412 ] ; 2000.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), CDC2-CDC28 Kinases (MeSH), Cell Cycle (MeSH), Cloning, Molecular (MeSH), Cyclin-Dependent Kinase 2 (MeSH), Cyclin-Dependent Kinases (genetics), Cyclin-Dependent Kinases (metabolism), Cyclins (chemistry), Cyclins (genetics), Cyclins (metabolism), Enzyme Activation (MeSH), Humans (MeSH), Molecular Sequence Data (MeSH), Oryza (cytology), Oryza (genetics), Oryza (metabolism), Phylogeny (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Trees (cytology), Trees (genetics), Trees (metabolism).
- MESH :
- chemical , chemistry : Cyclins, Recombinant Proteins.
- chemical , genetics : Cyclin-Dependent Kinases, Cyclins, Protein-Serine-Threonine Kinases.
- chemical , metabolism : Cyclin-Dependent Kinases, Cyclins, Protein-Serine-Threonine Kinases, Recombinant Proteins.
- chemical : CDC2-CDC28 Kinases, Cyclin-Dependent Kinase 2.
- cytology : Oryza, Trees.
- genetics : Oryza, Trees.
- metabolism : Oryza, Trees.
- Amino Acid Sequence, Animals, Cell Cycle, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phylogeny, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
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.
DOI: 10.1046/j.1365-313x.2000.00846.x
PubMed: 11029700
Links to Exploration step
pubmed:11029700Le document en format XML
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Schrader</name></author><author><name sortKey="Sandberg, G" sort="Sandberg, G" uniqKey="Sandberg G" first="G" last="Sandberg">G. Sandberg</name></author><author><name sortKey="Umeda, M" sort="Umeda, M" uniqKey="Umeda M" first="M" last="Umeda">M. Umeda</name></author><author><name sortKey="Uchimiya, H" sort="Uchimiya, H" uniqKey="Uchimiya H" first="H" last="Uchimiya">H. Uchimiya</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:11029700</idno><idno type="pmid">11029700</idno><idno type="doi">10.1046/j.1365-313x.2000.00846.x</idno><idno type="wicri:Area/Main/Corpus">004827</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004827</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.</title><author><name sortKey="Yamaguchi, M" sort="Yamaguchi, M" uniqKey="Yamaguchi M" first="M" last="Yamaguchi">M. Yamaguchi</name><affiliation><nlm:affiliation>Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Fabian, T" sort="Fabian, T" uniqKey="Fabian T" first="T" last="Fabian">T. Fabian</name></author><author><name sortKey="Sauter, M" sort="Sauter, M" uniqKey="Sauter M" first="M" last="Sauter">M. Sauter</name></author><author><name sortKey="Bhalerao, R P" sort="Bhalerao, R P" uniqKey="Bhalerao R" first="R P" last="Bhalerao">R P Bhalerao</name></author><author><name sortKey="Schrader, J" sort="Schrader, J" uniqKey="Schrader J" first="J" last="Schrader">J. Schrader</name></author><author><name sortKey="Sandberg, G" sort="Sandberg, G" uniqKey="Sandberg G" first="G" last="Sandberg">G. Sandberg</name></author><author><name sortKey="Umeda, M" sort="Umeda, M" uniqKey="Umeda M" first="M" last="Umeda">M. Umeda</name></author><author><name sortKey="Uchimiya, H" sort="Uchimiya, H" uniqKey="Uchimiya H" first="H" last="Uchimiya">H. Uchimiya</name></author></analytic><series><title level="j">The Plant journal : for cell and molecular biology</title><idno type="ISSN">0960-7412</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>CDC2-CDC28 Kinases (MeSH)</term><term>Cell Cycle (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Cyclin-Dependent Kinase 2 (MeSH)</term><term>Cyclin-Dependent Kinases (genetics)</term><term>Cyclin-Dependent Kinases (metabolism)</term><term>Cyclins (chemistry)</term><term>Cyclins (genetics)</term><term>Cyclins (metabolism)</term><term>Enzyme Activation (MeSH)</term><term>Humans (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oryza (cytology)</term><term>Oryza (genetics)</term><term>Oryza (metabolism)</term><term>Phylogeny (MeSH)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Saccharomyces cerevisiae (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Trees (cytology)</term><term>Trees (genetics)</term><term>Trees (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cyclins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cyclin-Dependent Kinases</term><term>Cyclins</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cyclin-Dependent Kinases</term><term>Cyclins</term><term>Protein-Serine-Threonine Kinases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>CDC2-CDC28 Kinases</term><term>Cyclin-Dependent Kinase 2</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Oryza</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oryza</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oryza</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Cycle</term><term>Cloning, Molecular</term><term>Enzyme Activation</term><term>Humans</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Saccharomyces cerevisiae</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11029700</PMID><DateCompleted><Year>2001</Year><Month>01</Month><Day>11</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>06</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0960-7412</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Oct</Month></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.</ArticleTitle><Pagination><MedlinePgn>11-20</MedlinePgn></Pagination><Abstract><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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yamaguchi</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fabian</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Sauter</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Bhalerao</LastName><ForeName>R P</ForeName><Initials>RP</Initials></Author><Author ValidYN="Y"><LastName>Schrader</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Sandberg</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Umeda</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Uchimiya</LastName><ForeName>H</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016213">Cyclins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="D042846">CDC2-CDC28 Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="C495894">CDK2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="D051357">Cyclin-Dependent Kinase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="D018844">Cyclin-Dependent Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="C066067">cyclin-dependent kinase-activating kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Plant J 2001 Feb;25(4):473</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042846" MajorTopicYN="Y">CDC2-CDC28 Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002453" MajorTopicYN="Y">Cell Cycle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051357" MajorTopicYN="N">Cyclin-Dependent Kinase 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018844" MajorTopicYN="N">Cyclin-Dependent Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016213" MajorTopicYN="N">Cyclins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>10</Month><Day>13</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>2</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>10</Month><Day>13</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11029700</ArticleId><ArticleId IdType="pii">tpj846</ArticleId><ArticleId IdType="doi">10.1046/j.1365-313x.2000.00846.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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