Alterations in the transport and processing of Rous sarcoma virus envelope glycoproteins mutated in the signal and anchor regions

John W. Wills, J. Marie Hardwick, Karen Shaw, Eric Hunter

Research output: Contribution to journalArticle

Abstract

The env gene of Rous sarcoma virus codes for two glycoproteins which are located on the surface of infectious virions. Subcloning of these coding sequences in the place of the late region of SV40 DNA has allowed the expression of a normally glycosylated, functionally active glycoprotein complex on the surface of monkey cells. Through the use of site‐directed mutagenesis, the role of specific amino acids in the signal peptide, signal peptidase cleavage site, and membrane anchor region have been investigated. Amino‐terminal mutations have shown that deletion of the signal peptidase cleavage site along with one or two amino acids of the hydrophobic signal peptide results in the synthesis of an unglycosylated. uncleaved, and presumably cytoplasmically located precursor. Nevertheless, changing the signal peptidase cleavage site from ala/asp to ala/asn does not block the translocation of the glycoprotein across the membrane or the action of the peptidase. At the other end of the molecule, carboxy‐terminal mutations have shown that the deletion of the hydrophobic membrane anchor region is not sufficient for the secretion of the truncated glycoprotein. Interpretations of these results based on recent models for protein transport and secretion are discussed.

Original languageEnglish (US)
Pages (from-to)81-94
Number of pages14
JournalJournal of cellular biochemistry
Volume23
Issue number1-4
DOIs
StatePublished - 1983

Keywords

  • Rous sarcoma virus
  • cleavage site mutants
  • deletion mutant
  • env gene mutants
  • membrane anchor region
  • signal peptide

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Alterations in the transport and processing of Rous sarcoma virus envelope glycoproteins mutated in the signal and anchor regions'. Together they form a unique fingerprint.

  • Cite this