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Activation of Ha-ras p21 by substitution, deletion, and insertion mutations.
Author(s) -
Randall G. Chipperfield,
Simon S. Jones,
K M Lo,
Robert A. Weinberg
Publication year - 1985
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.5.8.1809
Subject(s) - biology , point mutation , mutagenesis , genetics , mutation , residue (chemistry) , mutant , site directed mutagenesis , amino acid , microbiology and biotechnology , gene , biochemistry
The transforming activity of naturally arising ras oncogenes results from point mutations that affect residue 12 or 61 of the encoded 21-kilodalton protein (p21). By use of site-directed mutagenesis, we showed that deletions and insertions of amino acid residues in the region of residue 12 are also effective in conferring oncogenic activity on p21. Common to these various alterations is the disruption that they create in this domain of the protein, which we propose results in the inactivation of a normal function of the protein.

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