The Arabidopsis D-type Cyclins CycD2 and CycD3 Both Interact in Vivo with the PSTAIRE Cyclin-dependent Kinase Cdc2a but Are Differentially Controlled

D-type cyclins (CycD) play key roles in linking the Arabidopsis cell cycle to extracellular and developmental signals, but little is known of their regulation at the post-transcriptional level or of their cyclin-dependent kinase (CDK) partners. Using new antisera to CycD2 and CycD3, we demonstrate t...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-03, Vol.276 (10), p.7041-7047
Main Authors: Healy, J.M.Sandra, Menges, Margit, Doonan, John H., Murray, JamesA.H.
Format: Article
Language:English
Subjects:
Arabidopsis
Arabidopsis - chemistry
Arabidopsis Proteins
Blotting, Western
CDC2 Protein Kinase - chemistry
Cdc2a protein
CycD2 protein
CycD3 protein
Cyclin D3
cyclin-dependent kinase
Cyclin-Dependent Kinases - metabolism
Cyclins - metabolism
Kinetics
Models, Biological
Peptide Fragments - chemistry
Precipitin Tests
Protein Binding
Protein Biosynthesis
RNA, Messenger - metabolism
Sucrose - pharmacology
Time Factors
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Summary:D-type cyclins (CycD) play key roles in linking the Arabidopsis cell cycle to extracellular and developmental signals, but little is known of their regulation at the post-transcriptional level or of their cyclin-dependent kinase (CDK) partners. Using new antisera to CycD2 and CycD3, we demonstrate that the CDK partner of these Arabidopsiscyclins is the PSTAIRE-containing CDK Cdc2a. Previous analysis has shown that transcript levels of CycD2 and CycD3are regulated in response to sucrose levels and that both their mRNA levels and kinase activity are induced with different kinetics during the G1 phase of cells reentering the division cycle from quiescence (1). Here we analyze the protein levels and kinase activity of CycD2 and CycD3. We show that CycD3 protein and kinase activity parallel the abundance of its mRNA and that CycD3 protein is rapidly lost from cells in stationary phase or following sucrose removal. In contrast to both CycD3 and the regulation of its own mRNA levels, CycD2 protein is present at constant levels. CycD2 kinase activity is regulated by sequestration of CycD2 protein in a form inaccessible to immunoprecipitation and probably not complexed to Cdc2a.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M009074200