The viral SV40 T antigen cooperates with dj2 to enhance hsc70 chaperone function.
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.
Salma
Athanasia
A
Laboratory of General Biology, Medical School, University of Ioannina, Greece.
Tsiapos
Apostolos
A
Lazaridis
Ioannis
I
D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism / Q000502:physiology*; D019556:COS Cells; D002460:Cell Line; D002522:Chlorocebus aethiops; D050883:HSC70 Heat-Shock Proteins / Q000378:metabolism / Q000502:physiology*; D050956:HSP40 Heat-Shock Proteins / Q000502:physiology*; D047468:Immunoprecipitation; D051379:Mice; D041681:NIH 3T3 Cells; D011485:Protein Binding; D017510:Protein Folding
D000952:Antigens, Polyomavirus Transforming; C107481:DNAJA1 protein, human; D050883:HSC70 Heat-Shock Proteins; D050956:HSP40 Heat-Shock Proteins