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- W2083009248 abstract "Human adenovirus E1A proteins and oncogene products of several other DNA tumour viruses derive much of their oncogenic potential from interactions with cellular polypeptides. E1A proteins form complexes with p105 Rb and a related p107 polypeptide, and with at least three other proteins (p60 cycA , p130, and p300); all may be required for cell transformation. Using a series of E1A deletion mutants, we have carried out a quantitative analysis of the binding patterns of cellular proteins to E1A products. Binding of most of the proteins was affected at least partially by mutations within the amino terminal 25 residues, amino acids 36–69 within conserved region 1 (CR1), and residues 121–138 in conserved region 2 (CR2). However, the specific binding characteristics of each protein varied considerably. p300 was the only species for which binding was totally eliminated by deletions at the amino terminus. Removal of regions within CR1 eliminated binding of all species except p107 and p60 cycA . Deletion of portions of CR2 reduced or eliminated binding of all proteins except p300. Thus, whereas cellular polypeptides generally were found to interact with the same three regions of E1A proteins, specific interactions varied considerably.Key words: DNA tumour viruses, transformation, oncogenes, cell cycle, protein complexes." @default.
- W2083009248 created "2016-06-24" @default.
- W2083009248 creator A5009376139 @default.
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- W2083009248 creator A5023030692 @default.
- W2083009248 creator A5057466781 @default.
- W2083009248 date "1992-10-01" @default.
- W2083009248 modified "2023-10-16" @default.
- W2083009248 title "Quantitative analysis of regions of adenovirus E1A products involved in interactions with cellular proteins" @default.
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