title: The role of the J domain of SV40 large T in cellular transformation.
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.
authors.affiliation: Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, Massachusetts 02115, USA.
authors.forename: J A
authors.initials: JA
authors.lastname: DeCaprio
mesh_terms: D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites / Q000502:physiology; D002472:Cell Transformation, Viral; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D016160:Retinoblastoma Protein / Q000378:metabolism; D013539:Simian virus 40 / Q000276:immunology / Q000378:metabolism*
chemical_list: D000952:Antigens, Polyomavirus Transforming; D018840:HSP70 Heat-Shock Proteins; D016160:Retinoblastoma Protein