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

AUTOR(ES)

Trahey, M

RESUMO

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.

Documentos Relacionados

• Localisation of the human N-ras oncogene to chromosome 1cen - p21 by in situ hybridisation.
• Cellular N-Ras Promotes Cell Survival by Downregulation of Jun N-Terminal Protein Kinase and p38
• Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus.
• Activation of N-ras in a human melanoma cell line.
• Murine Leukemia Virus Proviral Insertions between the N-ras and unr Genes in B-Cell Lymphoma DNA Affect the Expression of N-ras Only