The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis

W G Dunphy1, L Brizuela, D Beach

  • 1Department of Biology, University of California, San Diego, La Jolla 92093.

Cell
|July 29, 1988
PubMed

Insights

The yeast suc1 gene product (p13) inhibits Xenopus maturation-promoting factor (MPF) by binding to it. This suggests p13 interacts with MPF components, including the Xenopus cdc2 protein.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Maturation-promoting factor (MPF) in Xenopus induces mitotic entry.
  • cdc2 kinase regulates mitotic initiation in fission yeast.
  • The yeast suc1 gene product (p13) interacts with cdc2 kinase.

Purpose of the Study:

  • To investigate the inhibitory effect of the yeast suc1 gene product (p13) on MPF in Xenopus egg extracts.
  • To determine the mechanism by which p13 inhibits MPF activity.

Main Methods:

  • Utilized cell-free extracts from Xenopus eggs.
  • Employed p13 affinity chromatography to isolate interacting proteins.
  • Assayed MPF activity in response to p13.

Main Results:

  • Yeast p13 potently inhibited MPF activity in Xenopus extracts.
  • p13 directly bound to MPF, leading to quantitative depletion of MPF activity.
  • The Xenopus cdc2 protein and a 42 kd protein were identified as MPF components binding to p13.

Conclusions:

  • The yeast suc1 gene product (p13) acts as an inhibitor of Xenopus MPF.
  • Xenopus cdc2 protein and a 42 kd protein are likely components of MPF.
  • These findings highlight conserved mechanisms in cell cycle regulation between yeast and Xenopus.

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