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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-05

AUTHORS

U. Strausfeld, J. C. Labbé, D. Fesquet, J. C. Cavadore, A. Picard, K. Sadhu, P. Russell, M. Dorée

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 (see refs 1 and 2 for review). The phos-phatase(s) involved in p34cdc2 dephosphorylation is unknown, but the product of the fission yeast cdc25+ gene3,4, and its homologues in budding yeast5 and Drosophila6 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. Addi-tion of the purified bacterially expressed product of the human homologue of the fission yeast cdc25+ gene7 (p54CDC25H) triggers p34cdc2 dephosphorylation and activates HI histone kinase activity in this preparation. We propose that the cdc25+ gene product directly activates the p34cdc2–cyclin B complex. More... »

PAGES

242-245

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/351242a0

DOI

http://dx.doi.org/10.1038/351242a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051804100

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1828290


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