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The viral SV40 T antigen cooperates with dj2 to enhance hsc70 chaperone function
Author(s) -
Salma Athanasia,
Tsiapos Apostolos,
Lazaridis Ioannis
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06019.x
Subject(s) - chaperone (clinical) , microbiology and biotechnology , function (biology) , virology , antigen , biology , chemistry , genetics , medicine , pathology
Simian virus 40 large T antigen is a J‐domain‐containing protein with multiple functions. Among its numerous activities, T antigen can bind heat shock cognate 70 (hsc70) but the biological significance of this interaction has not been fully understood. Here, we show that T antigen can act as an hsc70 co‐chaperone enhancing the protein‐folding ability of the hsc70 chaperone machine. We also show that T antigen exerts its function in collaboration with the mammalian homologue of DnaJ. Moreover, we show that the participation of T antigen in the hsc70 chaperone machine has cell‐type‐specific characteristics.