The viral SV40 T antigen cooperates with dj2 to enhance hsc70 chaperone function

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Updated: Jul 12, 2026

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome
05:22

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome

Published on: September 13, 2024

Athanasia Salma1, Apostolos Tsiapos, Ioannis Lazaridis

  • 1Laboratory of General Biology, Medical School, University of Ioannina, Greece.

The FEBS Journal
|September 1, 2007
PubMed

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.

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