Cell cycle-dependent association of Gag-Mil and hsp90.
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.
Lovrić
J
J
Max-Planck-Institut für Molekulare Genetik, Abt. Schuster, Berlin (Dahlem), Germany.
Bischof
O
O
Moelling
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002453:Cell Cycle; D002461:Cell Line, Transformed; D015683:Gene Products, gag / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D019908:Proto-Oncogene Proteins c-raf; D011784:Quail
D015683:Gene Products, gag; D006360:Heat-Shock Proteins; D011518:Proto-Oncogene Proteins; D017346:Protein Serine-Threonine Kinases; D019908:Proto-Oncogene Proteins c-raf