Phosphorylation and activation of 13S condensin by Cdc2 in vitro

Kimura, K., Hirano, M., Kobayashi, R., Hirano, T. (October 1998) Phosphorylation and activation of 13S condensin by Cdc2 in vitro. Science, 282 (5388). pp. 487-90. ISSN 0036-8075 (Print)

Abstract

13S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 13S condensin introduces positive supercoils into DNA in the presence of topoisomerase I and adenosine triphosphate in vitro. The supercoiling activity of 13Scondensin 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 13S 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 13Scondensin by Cdc2 may trigger mitotic chromosome condensation in vitro.

Item Type:	Paper
Uncontrolled Keywords:	Adenosinetriphosphatase/chemistry/ metabolism Amino Acid Sequence Animals CDC2 Protein Kinase/ metabolism Chromosomes/chemistry/ metabolism DNA, Circular/chemistry/metabolism DNA, Superhelical/ chemistry DNA-Binding Proteins/chemistry/ metabolism Enzyme Activation Interphase Mitosis Molecular Sequence Data Multiprotein Complexes Nucleic Acid Conformation Peptide Mapping Phosphorylation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Xenopus
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosome bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function > chromosome bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation organism description > animal > Frog > xenopus
CSHL Authors:	Hirano, Michiko Hirano, Tatsuya Kimura, Keiji Kobayashi, Ryuji
Communities:	CSHL labs > Hirano lab CSHL labs > Kobayashi lab
Depositing User:	Kathleen Darby
Date:	16 October 1998
Date Deposited:	01 May 2014 19:02
Last Modified:	01 May 2014 19:02
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/29903

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