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PMID: 9776252 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Molecular chaperone function of the SV40 large T antigen.

Developments in biological standardization ·Vol. 94 ·1998-00-00 ·Pages 313-9

Pipas JM

Abstract

The SV40 large T antigen (T antigen) is a potent viral oncogene capable of inducing tumours in test animals and transforming cells in culture. T antigen possesses multiple transforming functions that act in a cell-type dependent manner. One of these transforming functions requires a physical association between T antigen and the cellular tumour suppressor p53, while another requires T antigen binding to the retinoblastoma family of tumour suppressors. A third transforming function, <<Activity X>>, maps to the amino terminus of large T antigen, sequences also present in small t antigen. Our recent studies have shown that Activity X: (i) is a J-domain and that T antigen possesses the biochemical properties of a DnaJ molecular chaperone; (ii) must act in cis with the T antigen Rb-family binding motif to transform; and, (iii) must act in cis with some factor through its carboxy terminal half of T antigen, possibly p53, to transform.

MeSH Terms
Amino Acid Sequence Animals Antigens, Polyomavirus Transforming/physiology Cell Transformation, Neoplastic Humans Molecular Chaperones/physiology Molecular Sequence Data Protein Structure, Secondary Sequence Homology, Amino Acid Simian virus 40/pathogenicity
Chemicals
Antigens, Polyomavirus Transforming Molecular Chaperones
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Pipas J M
Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260, USA.
Article Info
Journal
Developments in biological standardization
Abbr.
Dev Biol Stand
ISSN
0301-5149
Published
1998-00-00
Pages
313-9
Language
English
Region
Switzerland
NLM ID
0427140
Subset
IM
Grants
NCI NIH HHS · CA40586 · United States
External Links
PubMed source
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