MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins

Genome Biol. 2004;5(3):R21. doi: 10.1186/gb-2004-5-3-r21. Epub 2004 Feb 13.

Abstract

We evaluated the evolutionary conservation of glycine myristoylation within eukaryotic sequences. Our large-scale cross-genome analyses, available as MYRbase, show that the functional spectrum of myristoylated proteins is currently largely underestimated. We give experimental evidence for in vitro myristoylation of selected predictions. Furthermore, we classify five membrane-attachment factors that occur most frequently in combination with, or even replacing, myristoyl anchors, as some protein family examples show.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence / genetics
  • Animals
  • Arabidopsis / genetics
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / physiology
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / chemistry
  • Caenorhabditis elegans Proteins / physiology
  • Conserved Sequence / genetics
  • Databases, Protein*
  • Drosophila / genetics
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / physiology
  • Evolution, Molecular
  • Genome*
  • Genome, Fungal
  • Genome, Human
  • Glycine / metabolism*
  • Humans
  • Mice
  • Myristic Acid / metabolism*
  • Proteins / chemistry*
  • Proteins / physiology*
  • Saccharomyces / genetics

Substances

  • Arabidopsis Proteins
  • Caenorhabditis elegans Proteins
  • Drosophila Proteins
  • Proteins
  • Myristic Acid
  • Glycine