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PMID: 1312880 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

cdc25+ encodes a protein phosphatase that dephosphorylates p34cdc2.

Molecular biology of the cell ·Vol. 3 ·No. 1 ·1992-01-00 ·Pages 73-84

Lee MS, Ogg S, Xu M, Parker LL, Donoghue DJ, Maller JL, Piwnica-Worms H

Abstract

To determine how the human cdc25 gene product acts to regulate p34cdc2 at the G2 to M transition, we have overproduced the full-length protein (cdc25Hs) as well as several deletion mutants in bacteria as glutathione-S-transferase fusion proteins. The wild-type cdc25Hs gene product was synthesized as an 80-kDa fusion protein (p80GST-cdc25) and was judged to be functional by several criteria: recombinant p80GST-cdc25 induced meiotic maturation of Xenopus oocytes in the presence of cycloheximide; p80GST-cdc25 activated histone H1 kinase activity upon addition to extracts prepared from Xenopus oocytes; p80GST-cdc25 activated p34cdc2/cyclin B complexes (prematuration promoting factor) in immune complex kinase assays performed in vitro; p80GST-cdc25 stimulated the tyrosine dephosphorylation of p34cdc2/cyclin complexes isolated from Xenopus oocyte extracts as well as from overproducing insect cells; and p80GST-cdc25 hydrolyzed p-nitrophenylphosphate. In addition, deletion analysis defined a functional domain residing within the carboxy-terminus of the cdc25Hs protein. Taken together, these results suggest that the cdc25Hs protein is itself a phosphatase and that it may function directly in the tyrosine dephosphorylation and activation of p34cdc2 at the G2 to M transition.

Related Genes
cdc25<up>+</up>
MeSH Terms
Animals Base Sequence CDC2 Protein Kinase/metabolism Cell Line Glutathione Transferase/metabolism Maturation-Promoting Factor/physiology Meiosis Molecular Sequence Data Nitrophenols/metabolism Oocytes/physiology Organophosphorus Compounds/metabolism Phosphoprotein Phosphatases/genetics,metabolism Phosphorylation Protein Biosynthesis Proteins/genetics,metabolism Recombinant Fusion Proteins/biosynthesis,metabolism Tyrosine/metabolism Xenopus cdc25 Phosphatases
Chemicals
Nitrophenols Organophosphorus Compounds Proteins Recombinant Fusion Proteins nitrophenylphosphate Tyrosine Glutathione Transferase CDC2 Protein Kinase Maturation-Promoting Factor Phosphoprotein Phosphatases cdc25 Phosphatases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lee M S
Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111.
Ogg S
Xu M
Parker L L
Donoghue D J
Maller J L
Piwnica-Worms H
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.3.1.73
Published
1992-01-00
Pages
73-84
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC275503
Subset
IM
Grants
NCI NIH HHS · CA 34456 · United States
NIGMS NIH HHS · GM26743 · United States
NHLBI NIH HHS · HL07053 · United States
External Links
PubMed source DOI: 10.1091/mbc.3.1.73 PMC Full Text View journal details
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