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Acylation: A new post‐translational modification specific for plasma membrane‐associated simian virus 40 large T‐antigen
Author(s) -
Klockmann Ulrich,
Deppert Wolfgang
Publication year - 1983
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(83)80081-7
Subject(s) - acylation , simian , antigen , virus , chemistry , virology , biology , biochemistry , immunology , catalysis
SV40 transformed mouse cells (mKSA) were labeled in parallel with either [ 35 S]methionine or [ 3 H]palmitate and subfractionated. Nuclear extracts and solubilized plasma membranes were analyzed for the presence of either 35 S‐ or 3 H‐labeled SV40 large tumor antigen by immunoprecipitation and SDS polyacrylamide gel electrophoresis. The majority of the [ 35 S]methionine labeled large T was recovered from the nuclear fraction, only minor amounts were detected in plasma membranes. In contrast, large T labeled specifically with [ 3 H]palmitate was found only in the plasma membrane fraction. Our results demonstrate a specific acylation of large T associated with plasma membranes, suggesting that the membrane location of this predominantly nuclear protein is specific.