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Phosphorylation and Activation of 13 S Condensin by Cdc2 in Vitro
Abstract
13 S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 13 S condensin introduces positive supercoils into DNA in the presence of topoisomerase I and adenosine triphosphate in vitro. The supercoiling activity of 13 S condensin was regulated by mitosis-specific phosphorylation. Immunodepletion, in vitro phosphorylation, and peptide-mapping experiments indicated that Cdc2 is likely to be the kinase that phosphorylates and activates 13 S condensin. Multiple Cdc2 phosphorylation sites are clustered in the carboxyl-terminal domain of the XCAP-D2 ( Xenopus chromosome-associated polypeptide D2) subunit. These results suggest that phosphorylation of 13 S condensin by Cdc2 may trigger mitotic chromosome condensation in vitro.
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Metadata
- Authors
- Kimura, K., Hirano, M., Kobayashi, R., & Hirano, T.
- Venue
- Science
- Published
- 1998-10-16
- Volume
- 282
- Issue
- 5388
- Pages
- 487-490
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1975622188
- Cited by
- 378
- References
- 0
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kimura, K., Hirano, M., Kobayashi, R., & Hirano, T. (1998). Phosphorylation and Activation of 13 S Condensin by Cdc2 in Vitro. Science. https://doi.org/10.1126/science.282.5388.487
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