Abstract:
:We have partially purified a specific cyclin B2 kinase (cyk) from prophase oocytes of Xenopus laevis after an ATP-gamma-S activation step. Phosphopeptide analysis identified Ser53 as the major in vitro phosphorylation site for cyk in cyclin B2. Using a synthetic peptide derived from cyclin B2 encompassing Ser53 (cyktide) as a substrate, cyk was shown to be activated during progesterone-induced maturation, with a peak of activity between 40 and 50% maturation. A sustained high cyk activity was observed in oscillating egg extracts. Microinjection of cyk-phosphorylated cyclin B2 into prophase oocytes accelerated progesterone-induced maturation by about 2 h, indicating that cyclin B2 is a relevant substrate for cyk and that the function of cyk is situated upstream of cdc2-cyclin B activation. Microinjection of cyk-phosphorylated cyktide or a combination of cyk and cyclin B1 into G2 fibroblasts induced significant changes in cell morphology, reminiscent of a premature prophase-like phenotype. Similarly, addition of cyk-phosphorylated cyktide in cyclin B1-dependent interphase extracts resulted in histone H1 kinase activation.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Derua R,Stevens I,Waelkens E,Fernandez A,Lamb N,Merlevede W,Goris Jdoi
10.1006/excr.1996.3436subject
Has Abstractpub_date
1997-02-01 00:00:00pages
310-24issue
2eissn
0014-4827issn
1090-2422pii
S0014-4827(96)93436-9journal_volume
230pub_type
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更新日期:1998-08-25 00:00:00
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