A single point mutation has pleiotropic effects on pp60v-src function

  • Welham M
  • Wyke J
39Citations
Citations of this article
13Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The Rous sarcoma virus mutant tsLA29 encodes a pp60v-src molecule that is temperature sensitive for both tyrosine kinase activity and its ability to locate at the cell periphery. The defect in localization appears to be due to a perturbation in events following complex dissociation, since the mutant enzyme shows a rapidly reversible association with the cytoskeleton when shifted between permissive and restrictive temperatures. Although tsLA29 pp60v-src differs from the wild type at three amino acid residues, studies with chimeric proteins show that only one of the mutations, an alanine-for-proline substitution at residue 507, accounts for all the temperature-sensitive characteristics. Moreover, a single second site mutation, at residue 427, can restore the wild phenotype. Cells infected with a chimeric virus encoding only the alanine substitution at position 507 have a conspicuously fusiform morphology, suggesting that this mutation also has subtle effects on pp60v-src function that are apparently compensated for by the other mutations in native tsLA29.

Cite

CITATION STYLE

APA

Welham, M. J., & Wyke, J. A. (1988). A single point mutation has pleiotropic effects on pp60v-src function. Journal of Virology, 62(6), 1898–1906. https://doi.org/10.1128/jvi.62.6.1898-1906.1988

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free