Abstract
In the fission yeast S. pombe, the Mr = 34 kd product of the cdc2+ gene (p34cdc2) is a protein kinase that controls entry into mitosis. In Xenopus oocytes and other cells, maturation-promoting factor (MPF) appears in late G2 phase and is able to cause entry into mitosis. Purified MPF consists of two major proteins of Mr ≈ 32 kd and 45 kd and expresses protein kinase activity. We report here that antibodies to S. pombe p34cdc2 are able to immunoblot and immunoprecipitate the ≈32 kd component of MPF from Xenopus eggs. The Mr ≈ 32 kd and 45 kd proteins exist as a complex that expresses protein kinase activity. These findings indicate that a Xenopus p34cdc2 homolog is present in purified MPF and suggest that p34cdc2 is a component of the control mechanism initiating mitosis generally in eukaryotic cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 433-439 |
| Number of pages | 7 |
| Journal | Cell |
| Volume | 54 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 29 1988 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology
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