Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes

Protein Eng. 2001 Jan;14(1):17-25. doi: 10.1093/protein/14.1.17.

Abstract

To investigate the occurrence of glycosylphosphatidylinositol (GPI) lipid anchor modification in various taxonomic ranges, potential substrate proteins have been searched for in completely sequenced genomes. We applied the big-pi predictor for the recognition of propeptide cleavage and anchor attachment sites with a new, generalized analytical form of the extreme-value distribution for evaluating false-positive prediction rates. (i) We find that GPI modification is present among lower and higher Eukaryota (approximately 0.5% of all proteins) but it seems absent in all eubacterial and three archaeobacterial species studied. Four other archaean genomes appear to encode such a fraction of substrate proteins (in the range of eukaryots) that they cannot be explained as false-positive predictions. This result supports the possible existence of GPI anchor modification in an archaean subgroup. (ii) The frequency of GPI-modified proteins on various chromosomes of a given eukaryotic species is different. (iii) Lists of potentially GPI-modified proteins in complete genomes with their predicted cleavage sites are available at http://mendel.imp.univie.ac.at/gpi/gpi_genomes.html. (iv) Orthologues of known transamidase subunits have been found only for EUKARYA: Inconsistencies in domain structure among homologues some of which may indicate sequencing errors are described. We present a refined model of the transamidase complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea
  • Archaeal Proteins / chemistry
  • Bacteria
  • Cell Adhesion Molecules / chemistry
  • Eukaryotic Cells
  • Evolution, Molecular*
  • Genome
  • Glycosylphosphatidylinositols / classification*
  • Glycosylphosphatidylinositols / genetics*
  • Humans
  • Mathematics
  • Membrane Glycoproteins / chemistry
  • Molecular Sequence Data
  • Mutation
  • Phylogeny
  • Protein Isoforms
  • Protein Precursors / chemistry
  • Protein Processing, Post-Translational*
  • Protozoan Proteins / chemistry
  • Sequence Analysis, Protein / methods
  • Transaminases / chemistry

Substances

  • Archaeal Proteins
  • Cell Adhesion Molecules
  • GPAA1 protein, human
  • Glycosylphosphatidylinositols
  • Membrane Glycoproteins
  • PIGK protein, human
  • Protein Isoforms
  • Protein Precursors
  • Protozoan Proteins
  • Transaminases

Associated data

  • SWISSPROT/P08198