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Acylated simian virus 40 large T‐antigen: a new subclass associated with a detergent‐resistant lamina of the plasma membrane.
Author(s) -
Klockmann U.,
Deppert W.
Publication year - 1983
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1983.tb01560.x
Subject(s) - membrane , biology , antigen , virus , microbiology and biotechnology , lamina , subclass , biophysics , virology , biochemistry , antibody , immunology , anatomy
We have analyzed the plasma membrane association of the SV40 large tumor antigen (large T) in SV40‐transformed BALB/c mouse tumor cells (mKSA). Isolated plasma membranes were subfractionated: treatment with the non‐ionic detergent Nonidet P40 (NP40) resulted in a NP40‐resistant plasma membrane lamina, which could be further extracted with the zwitterionic detergent Empigen BB. Analysis of the different plasma membrane fractions revealed that only about one third of large T associated with isolated plasma membranes could be solubilized with NP40. The residual plasma membrane‐associated large T was tightly bound to the NP40‐resistant lamina of the plasma membrane from which it was released by treatment with the zwitterionic detergent Empigen BB. Further evidence for a specific interaction of a distinct subclass of large T with the plasma membrane was provided by showing that only T associated with the NP40‐resistant lamina of the plasma membrane contained covalently bound fatty acid. Neither nuclear large T nor large T in the NP40‐soluble plasma membrane fraction could be labeled with [3H]palmitic acid. Our results indicate that an acylated subclass of large T interacts specifically with a structure of the plasma membrane, suggesting that it might be involved in a membrane‐dependent biological function.