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Relationship of phosphorylation to the oligomerization of SV40 T antigen and its association with p53
Author(s) -
Stürzbecher Horst-Werner,
Mörike Martin,
Montenarh Mathias,
Henning Roland
Publication year - 1985
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(85)81087-5
Subject(s) - dephosphorylation , phosphorylation , antigen , chemistry , phosphatase , sv40 large t antigen , microbiology and biotechnology , enzyme , biochemistry , biology , immunology , gene , transfection
The potential significance of the phosphorylation of SV40 large T antigen for oligomers and complexes with the cellular protein p53 was investigated. We observed that T antigen oligomers remain stable after enzymatic dephosphorylation by alkaline phosphatase up to 80%. Separate analysis of free and p53‐bound T antigen revealed a considerably lower phosphorylation of the p53‐bound subclass. Therefore, a simple correlation between the overall phosphorylation of T antigen and the formation of oligomers and T‐p53 complexes is highly unlikely.