DING proteins are from Pseudomonas

FEMS Microbiol Lett. 2005 Nov 15;252(2):215-22. doi: 10.1016/j.femsle.2005.08.047. Epub 2005 Sep 15.

Abstract

DING proteins have been described as animal and plant proteins with potential biomineralisation, receptor or signalling roles that have been characterised by an N-terminal DINGGG-sequence. However, these sequences have only ever been identified as either N-terminal peptides or partial cDNA sequences, and have yet to be detected in any of the many genomic animal and plant genomes now available. Microbial relatives of the DING proteins have been described, which appear to be periplasmic phosphate-binding proteins. Recently, full-length Pseudomonas aeruginosa UCBPP-PA14 and Hypericum perforatum genes have been sequenced that show high homology to the published DING protein N-terminal sequences, and small peptides previously identified in conjunction with the peptide sequencing of DING proteins can also be mapped to regions across these full-length sequences. Searching with these sequences identifies other plant and animal cDNA fragments in the public nucleotide databases, and, additionally, an unordered rat genomic contig that contains a DING-like sequence on a small fragment. Analysing the codon usage of these DNA sequences identifies all of these sequences as of Pseudomonas origin, suggesting that DING proteins do not exist in eukaryotes, but instead are potentially due to microbial contamination or infection.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Codon / genetics
  • Computational Biology
  • Genome*
  • Hypericum / genetics
  • Molecular Sequence Data
  • Phylogeny
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Pseudomonas aeruginosa / chemistry
  • Pseudomonas aeruginosa / genetics*
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Codon
  • Plant Proteins