Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits.

@article{Kobayashi1992IdentificationOT,
  title={Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits.},
  author={Hideki Kobayashi and Elspeth Stewart and Randy YC Poon and J{\"o}rg P. Adamczewski and Julian Gannon and Tim Hunt},
  journal={Molecular biology of the cell},
  year={1992},
  volume={3 11},
  pages={
          1279-94
        }
}
The binding of cyclin A to p34cdc2 and p32cdk2 and the protein kinase activity of the complexes has been measured by cell-free translation of the corresponding mRNA in extracts of frog eggs, followed by immunoprecipitation. A variety of mutant cyclin A molecules have been constructed and tested in this assay. Small deletions and point mutations of highly conserved residues in the 100-residue "cyclin box" abolish binding and activation of both p34cdc2 and p32cdk2. By contrast, large deletions at… CONTINUE READING