Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth

Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3229-33. doi: 10.1073/pnas.92.8.3229.

Abstract

To complete the molecular characterization of coatomer, the preformed cytosolic complex that is involved in the formation of biosynthetic transport vesicles, we have cloned and characterized the gene for non-clathrin-coat protein alpha (alpha-COP) from Saccharomyces cerevisiae. The derived protein, molecular weight of 135,500, contains four WD-40 repeated motifs (Trp/Asp-containing motifs of approximately 40 amino acids). Disruption of the yeast alpha-COP gene is lethal. Comparison of the DNA-derived primary structure with peptides from bovine alpha-COP shows a striking homology. alpha-COP is localized to coated transport vesicles and coated buds of Golgi membranes derived from CHO cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Biological Transport
  • Cell Compartmentation
  • Cloning, Molecular
  • Coated Vesicles / physiology*
  • Coatomer Protein
  • Fungal Proteins / genetics*
  • Genes, Fungal / genetics*
  • Membrane Proteins / genetics*
  • Membrane Proteins / immunology
  • Membrane Proteins / isolation & purification
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Mutation
  • Restriction Mapping
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Coatomer Protein
  • Fungal Proteins
  • Membrane Proteins

Associated data

  • GENBANK/X83754