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

被引:48
作者
DeCaprio, JA [1 ]
机构
[1] Harvard Univ, Sch Med, Dana Farber Canc Inst, Boston, MA 02115 USA
关键词
D O I
10.1006/biol.1998.0173
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1999 The International Association for Biologicals.
引用
收藏
页码:23 / 28
页数:6
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