Open AccessIn vitro mutagenesis of the v-sis transforming gene defines functional domains of its growth factor-related product.
Author(s) -
C. Richter King,
N. A. Giese,
Keith C. Robbins,
S A Aaronson
Publication year - 1985
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.16.5295
Subject(s) - gene product , gene , biology , mutagenesis , peptide sequence , mutant , transforming growth factor , function (biology) , mutation , microbiology and biotechnology , genetics , gene expression
The polypeptide sequence of the v-sis transforming gene product of simian sarcoma virus (SSV) can be divided into four regions that are likely to represent structural domains of the protein. Mutations were generated in the SSV nucleotide sequence to assay the extent or function of each of these regions. The results indicate that the helper virus-derived amino-terminal sequence as well as a core region homologous to polypeptide chain 2 of platelet-derived growth factor (PDGF) are required for the transforming function of the protein. Products of transforming but not nontransforming mutants formed dimer structures conformationally analogous to biologically active PDGF.
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