Transfer of glycosyl-phosphatidylinositol membrane anchors to polypeptide acceptors in a cell-free system. Academic Article uri icon

Overview

MeSH

  • Adenosine Triphosphate
  • Animals
  • Cell-Free System
  • Endoplasmic Reticulum
  • Glycosylation
  • Glycosylphosphatidylinositols
  • Guanosine Triphosphate
  • Protein Biosynthesis
  • Trypanosoma brucei brucei

MeSH Major

  • Glycolipids
  • Phosphatidylinositols
  • Variant Surface Glycoproteins, Trypanosoma

abstract

  • Glycosylinositol phospholipid (GPI) membrane anchors are the sole means of membrane attachment of a large number of cell surface proteins, including the variant surface glycoproteins (VSGs) of the parasitic protozoan, Trypanosoma brucei. Biosynthetic data suggest that GPI-anchored proteins are synthesized with carboxy-terminal extensions that are immediately replaced by GPI, suggesting the existence of preformed GPI species available for transfer to the nascent protein in the ER. Candidate precursor glycolipids having a linear sequence indistinguishable from the conserved core structure found on all GPI anchors, have been characterized in T. brucei. In this paper we describe the transfer of three GPI variants to endogenous VSG in vitro. GPI addition is not reduced by inhibitors of protein synthesis and does not require ATP or GTP, consistent with a transpeptidation mechanism.

publication date

  • July 1991

has subject area

  • Adenosine Triphosphate
  • Animals
  • Cell-Free System
  • Endoplasmic Reticulum
  • Glycolipids
  • Glycosylation
  • Glycosylphosphatidylinositols
  • Guanosine Triphosphate
  • Phosphatidylinositols
  • Protein Biosynthesis
  • Trypanosoma brucei brucei
  • Variant Surface Glycoproteins, Trypanosoma

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2289052

PubMed ID

  • 1828808

Additional Document Info

start page

  • 61

end page

  • 71

volume

  • 114

number

  • 1