Phosphorylation and activation of 13S condensin by Cdc2 in vitro

Science. 1998 Oct 16;282(5388):487-90. doi: 10.1126/science.282.5388.487.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Animals
  • CDC2 Protein Kinase / metabolism*
  • Chromosomes / chemistry
  • Chromosomes / metabolism*
  • DNA, Circular / chemistry
  • DNA, Circular / metabolism
  • DNA, Superhelical / chemistry*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Enzyme Activation
  • Interphase
  • Mitosis*
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Nucleic Acid Conformation
  • Peptide Mapping
  • Phosphorylation
  • Xenopus


  • DNA, Circular
  • DNA, Superhelical
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • condensin complexes
  • CDC2 Protein Kinase
  • Adenosine Triphosphatases

Associated data

  • GENBANK/AF067969