Open AccessDefinition of the minimal simian virus 40 large T antigen- and adenovirus E1A-binding domain in the retinoblastoma gene product.
Author(s) -
William G. Kaelin,
Mark E. Ewen,
David M. Livingston
Publication year - 1990
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.10.7.3761
Subject(s) - biology , mutant , gene product , microbiology and biotechnology , mastadenovirus , retinoblastoma , transformation (genetics) , gene , binding site , retinoblastoma protein , binding domain , virus , dna binding protein , adenoviridae , virology , recombinant dna , genetics , gene expression , transcription factor , cell cycle
It has previously been demonstrated that the simian virus 40 large T antigen and adenovirus E1A proteins can form complexes with the retinoblastoma susceptibility gene product (RB). We studied the ability of these proteins to bind to mutant RB proteins in vitro. A region of RB spanning residues 379 to 792 was found to be both necessary and sufficient for binding to T or E1A. Furthermore, this region of RB contains sufficient structural information to mimic wild-type RB in its ability to distinguish between wild-type T and the transformation-defective T mutant K1. The results of competition experiments with peptide analogs of the RB-binding sequence in T suggest that this region of RB makes direct contact with a short colinear region of T, i.e., residues 102 to 115, previously implicated in both transformation and RB binding.