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Updated: Aug 8, 2026

Studying Proteolysis of Cyclin B at the Single Cell Level in Whole Cell Populations
Published on: September 17, 2012
Cell cycle-dependent association of Gag-Mil and hsp90
J Lovrić1, O Bischof, K Moelling
1Max-Planck-Institut für Molekulare Genetik, Abt. Schuster, Berlin (Dahlem), Germany.
Abstract:
Immunoprecipitated p100Gag-Mil protein kinase from MH2-transformed quail embryo fibroblasts is associated with an 89 kDa protein. The molar ratio between p89 and Gag-Mil in the immunocomplex is 0.72, indicating that the majority of Gag-Mil is complexed with p89. During mitosis part of Gag-Mil is shifted to a form with reduced electrophoretic mobility, p102Gag-Mil. Appearance of p102Gag-Mil leads to a reduced association with p89 indicating that p102 is not associated with p89. Microsequencing of p89 isolated from immunoprecipitates of Gag-Mil identified the protein as the quail homologue of chicken hsp90. Our results show that p100Gag-Mil is associated with hsp90 with a high stoichiometry and that upshifted p102Gag-Mil is released from the complex with hsp90.
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