Structural characteristics of genomic islands associated with GMP synthases as integration hotspot among sequenced microbial genomes

Comput Biol Chem. 2012 Feb:36:62-70. doi: 10.1016/j.compbiolchem.2012.01.001. Epub 2012 Jan 12.

Abstract

tRNA, tmRNA and some small RNA genes are recognized as general integration hotspots of genomic islands (GIs). The GMP synthase gene (guaA) has been firstly identified as one insertion hotspot of foreign DNA fragments. Thirty four islands integrated into the guaA genes were identified in the 987 completely sequenced archaeal and bacterial genomes. These alien islands were widely distributed within the host strains belonging to Proteobacteria, Firmicutes and Actinobacteria. The analysis of structural characteristics of these GIs is important for further determination of the island mobility and transference into suitable hosts. The putative functional integrases encoded by guaA-associated islands were mainly composed of phage P4 integrases, and followed by phage PhiLC3 integrases. Interestingly, island-encoding AlpA is close to P4 integrase and is deduced to be the positive transcriptional regulatory factor of P4 integrase while the XRE protein is close to PhiLC3 integrase and may be the negative transcriptional regulatory factor of PhiLC3 integrase. An 8-bp consensus sequence (5'-GAGTGGGA-3') within the direct repeats of these GIs is the cutting site of the P4 integrases encoding by guaA-associated islands, in which the third nucleotide (G) is the key site. The large-scale investigation of the content of GMP synthase gene hotspots may be useful to find important functional islands within members of many key bacterial species and to transfer useful islands into more suitable hosts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / genetics
  • Bacterial Proteins / genetics
  • Base Sequence
  • Carbon-Nitrogen Ligases / genetics*
  • Consensus Sequence
  • Genome, Archaeal*
  • Genome, Bacterial*
  • Genomic Islands*
  • Molecular Sequence Data

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Carbon-Nitrogen Ligases
  • GMP synthase (glutamine-hydrolyzing)