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PMID: 10441399 Published · ppublish English Journal Article Review

The role of the J domain of SV40 large T in cellular transformation.

DeCaprio JA

Abstract

SV40 large T antigen (TAg)-mediated transformation is dependent on binding to p53 and the retinoblastoma tumor suppressor protein (pRB) and inactivating their growth suppressive functions. Transformation minimally requires three regions of TAg: a C-terminal domain that mediates binding to p53; the LXCXE motif (residues 103-107), necessary for binding to pRB and the related proteins p107 and p130; and an N-terminal domain (residues 1-82) that contains homology to the J domain found in cellular DnaJ/Hsp40 molecular chaperone proteins. We have found that the N-terminal J domain of T Ag cooperates with the LXCXE motif to inactivate the growth suppressive functions of the pRB-related proteins.

MeSH Terms
Animals Antigens, Polyomavirus Transforming/chemistry,metabolism Binding Sites/physiology Cell Transformation, Viral HSP70 Heat-Shock Proteins/metabolism Humans Protein Binding Retinoblastoma Protein/metabolism Simian virus 40/immunology,metabolism
Chemicals
Antigens, Polyomavirus Transforming HSP70 Heat-Shock Proteins Retinoblastoma Protein
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
DeCaprio J A
Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, Massachusetts 02115, USA.
Article Info
Journal
Biologicals : journal of the International Association of Biological Standardization
Abbr.
Biologicals
ISSN
1045-1056
Published
1999-03-00
Pages
23-8
Language
English
Region
England
NLM ID
9004494
Subset
IM
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