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Cell cycle‐dependent association of Gag‐Mil and hsp90
Author(s) -
Lovrić Josip,
Bischof Oliver,
Moelling Karin
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80598-9
Subject(s) - quail , chemistry , hsp90 , biochemistry , microbiology and biotechnology , glycoprotein , biology , heat shock protein , gene , endocrinology
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.