The Xenopus Cdc2 Protein Is a Component of Mpf, a Cytoplasmic Regulator of Mitosis

Dunphy, W. G., Brizuela, L., Beach, D., Newport, J. (July 1988) The Xenopus Cdc2 Protein Is a Component of Mpf, a Cytoplasmic Regulator of Mitosis. Cell, 54 (3). pp. 423-431. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/3293802
DOI: 10.1016/0092-8674(88)90205-X

Abstract

In Xenopus, a cytoplasmic agent known as MPF induces entry into mitosis. In fission yeast, genetic studies have shown that the cdc2 kinase regulates mitotic initiation. The 13 kd product of the suc1 gene interacts with the cdc2 kinase in yeast cells. We show that the yeast suc1 gene product (p13) is a potent inhibitor of MPF in cell-free extracts from Xenopus eggs. p13 appears to exert its antagonistic effect by binding directly to MPF. MPF activity is quantitatively depleted by chromatography on a p13 affinity column. Concomitantly, the Xenopus counterpart of the yeast cdc2 protein is adsorbed to the column. A 42 kd protein also binds specifically to the p13 affinity matrix. These findings suggest that the Xenopus cdc2 protein and the 42 kd protein are components of MPF.

Item Type: Paper
Subjects: organs, tissues, organelles, cell types and functions > organelles, types and functions > mitosis
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > Protein kinase C
organism description > animal > Frog > xenopus
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Gail Sherman
Date: 29 July 1988
Date Deposited: 17 Oct 2017 17:13
Last Modified: 17 Oct 2017 17:13
Related URLs:
URI: https://repository.cshl.edu/id/eprint/35140

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