NDLI: Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

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Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

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Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sigal, I. S. Wolanski, B. S. Temeles, G. L. Scolnick, E. M. D'alonzo, J. S. Socher, S. H. Gibbs, J. B.
Abstract	We report that residues Lys-16 and Asp-119 play critical roles in the guanine nucleotide binding and, consequently, the biological function of the Ha-ras-encoded protein (Ha). Substitution of an asparagine residue for Lys-16 reduces the affinity of Ha for GDP and GTP by a factor of 100 but does not alter the specificity of nucleotide binding. The replacement of Asp-119 with an alanine residue reduces the affinity of Ha for GDP and GTP by a factor of 20 and reduces the relative affinity of Ha for GDP over IDP from 200-500 to 10. Based on these observations, a structural model for the GDP/GTP-binding site of Ha is proposed. By microinjecting purified proteins into NIH 3T3 cells, we observed that the ability of [Ala119]Ha to induce changes characteristic of cellular transformation was much greater than that of normal Ha and similar to that of the oncogenic [Val12, Thr59]Ha. In this assay, [Asn16]Ha and [Val12, Asn16, Thr59]Ha were similar in potency to normal Ha. In yeast cells, Ha proteins with reduced nucleotide affinity exert a dominant temperature-dependent lethality that is avoided by the coexpression of the activated yeast ras gene [Ala18, Val19]RAS2. We interpret the biological consequences of reducing the nucleotide affinity of ras proteins in terms of two opposing factors: a growth-promoting effect, resulting from an increase in the GDP-GTP exchange rate, and a growth-limiting effect, resulting from an increase in the nucleotide-free ras protein species.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Guanine Nucleotides Metabolism Guanosine Diphosphate Guanosine Triphosphate Membrane Proteins Genetics Neoplasm Proteins Animals Binding Sites Cells, Cultured Escherichia Coli Fibroblasts Genes, Dominant Mice Mutation Proto-Oncogene Proteins P21(ras) Recombinant Proteins Saccharomyces Cerevisiae Substrate Specificity Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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