Phosphorylation of nonhistone proteins during premature chromosome condensation in a temperature-sensitive mutant, tsBN2.
- 1 January 1985
- journal article
- research article
- Published by Japan Society for Cell Biology in Cell Structure and Function
- Vol. 10 (3) , 259-270
- https://doi.org/10.1247/csf.10.259
Abstract
In tsBN2 cells, a temperature-sensitive (ts) mutant of the BHK21 cell line, with a ts-defect in its regulatory system for chromosome condensation, antigens that react with mitotic specific mouse monoclonal antibody MPM-2 were produced when premature chromosome condensation (PCC) was induced by a temperature shift. The polypeptides of antigens recognized by MPM-2 in tsBN2 cells with PCC were identical to those of antigens in mitotic cells. These antigens appeared concomitantly with chro-mosome condensation, which suggests that these mitotic-specific antigens may be related to chromosome condensation. As the production of mitotic-specific antigens was inhibited by W-7, a specific and potent antagonist of calmodulin, calmodulin may function in the mitotic phosphorylation of nonhistone protein.This publication has 1 reference indexed in Scilit:
- Analysis of proteins associated with chromosome condensation in baby hamster kidney cells.Journal of Biological Chemistry, 1984