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Journal of Virology, October 2003, p. 10706-10713, Vol. 77, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.19.10706-10713.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Simian Virus 40 T Antigens and J Domains: Analysis of Hsp40 Cochaperone Functions in Escherichia coli

Pierre Genevaux,1 Florence Lang,1 Françoise Schwager,1 Jai V. Vartikar,2 Kathleen Rundell,3 James M. Pipas,2 Costa Georgopoulos,1 and William L. Kelley1*

Département de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Genève 14, Switzerland,1 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260,2 Department of Microbiology-Immunology, Robert H. Lurie Comprehensive Cancer Center, Northwestern University, Chicago, Illinois 606113

Received 31 March 2003/ Accepted 10 July 2003

The N-terminal exon of DNA tumor virus T antigens represents a J domain that can direct interaction with the host-encoded Hsp70 chaperones. We have taken advantage of rapid Hsp40 cochaperone assays with Escherichia coli to assess simian virus 40 (SV40)-encoded J-domain loss of function. We found a strong correlation between loss of cochaperone function in E. coli and defective SV40 growth, suggesting that the major role of the J domain in DNA tumor viruses is to provide cochaperone function. We also report the expression of native SV40 virus T antigens in E. coli. Our results show that small t antigen, but not large T antigen (LT) or LT truncation TN125 or TN136, can functionally replace under limited growth conditions DnaJ (Hsp40) function in vivo. In addition, purified small t antigen can efficiently stimulate E. coli DnaK's (Hsp70) ATPase in vitro, thus behaving like a bona fide cochaperone. Furthermore, small t amino acids 83 to 174, which are adjacent to the viral J domain, can replace the E. coli DnaJ J-domain glycine-phenylalanine-rich domain, immediately adjacent to the J-domain sequences, even in the absence of significant amino acid similarity to their DnaJ counterpart. Taken together, our studies demonstrate that functionally related Hsp40 proteins from mammalian viral systems can be rapidly studied in bacteria and exploited to probe the universally conserved Hsp70 chaperone machine mechanism.

* Corresponding author. Present address: Division des Maladies Infectieuses, Hôpital Cantonal de Genève, 24, rue Micheli-du-Crest, CH-1211 Geneva 14, Switzerland. Phone: 41 22 372 9819. Fax: 41 22 372 9830. E-mail: william.kelley{at}hcuge.ch.

Journal of Virology, October 2003, p. 10706-10713, Vol. 77, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.19.10706-10713.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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