Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein.

Abstract:

:Oocytes arrested in the G2 phase of the cell cycle contain a p34cdc2/cyclin B complex which is kept in an inactive form by phosphorylation of its p34cdc2 subunit on tyrosine, threonine and perhaps serine residues. The phosphatase(s) involved in p34cdc2 dephosphorylation is unknown, but the product of the fission yeast cdc25+ gene, and its homologues in budding yeast and Drosophila are probably positive regulators of the transition from G2 to M phase. We have purified the inactive p34cdc2/cyclin B complex from G2-arrested starfish oocytes. Addition of the purified bacterially expressed product of the human homologue of the fission yeast cdc25+ gene (p54CDC25H) triggers p34cdc2 dephosphorylation and activates H1 histone kinase activity in this preparation. We propose that the cdc25+ gene product directly activates the p34cdc2-cyclin B complex.

journal_name

Nature

journal_title

Nature

authors

Strausfeld U,Labbé JC,Fesquet D,Cavadore JC,Picard A,Sadhu K,Russell P,Dorée M

doi

10.1038/351242a0

subject

Has Abstract

pub_date

1991-05-16 00:00:00

pages

242-5

issue

6323

eissn

0028-0836

issn

1476-4687

journal_volume

351

pub_type

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