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PMID: 3550423 Published · ppublish English Journal Article

Biochemical and biological properties of the human N-ras p21 protein.

Molecular and cellular biology ·Vol. 7 ·No. 1 ·1987-01-00 ·Pages 541-4

Trahey M, Milley RJ, Cole GE, Innis M, Paterson H, Marshall CJ, Hall A, McCormick F

Abstract

We characterized the normal (Gly-12) and two mutant (Asp-12 and Val-12) forms of human N-ras proteins produced by Escherichia coli. No significant differences were found between normal and mutant p21 proteins in their affinities for GTP or GDP. Examination of GTPase activities revealed significant differences between the mutant p21s: the Val-12 mutant retained 12% of wild-type GTPase activity, whereas the Asp-12 mutant retained 43%. Both mutant proteins, however, were equally potent in causing morphological transformation and increased cell motility after their microinjection into quiescent NIH 3T3 cells. This lack of correlation between transforming potency and GTPase activity or guanine nucleotide binding suggests that position 12 mutations affect other aspects of p21 function.

MeSH Terms
Animals Cell Transformation, Neoplastic Cells, Cultured Escherichia coli/genetics GTP Phosphohydrolases/metabolism Guanosine Diphosphate/metabolism Guanosine Triphosphate/metabolism Humans Mice Mutation Oncogenes Protein Binding Proto-Oncogene Proteins/genetics,metabolism Proto-Oncogene Proteins p21(ras)
Chemicals
Proto-Oncogene Proteins Guanosine Diphosphate Guanosine Triphosphate GTP Phosphohydrolases HRAS protein, human Proto-Oncogene Proteins p21(ras)
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Trahey M
Milley R J
Cole G E
Innis M
Paterson H
Marshall C J
Hall A
McCormick F
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36 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.7.1.541-544.1987
Published
1987-01-00
Pages
541-4
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365100
Subset
IM
External Links
PubMed source DOI: 10.1128/mcb.7.1.541-544.1987 PMC Full Text View journal details
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