Molecular identification of aiiA homologous gene from endophytic Enterobacter species and in silico analysis of putative tertiary structure of AHL-lactonase

P S Rajesh; V Ravishankar Rai

doi:10.1016/j.bbrc.2013.11.101

Molecular identification of aiiA homologous gene from endophytic Enterobacter species and in silico analysis of putative tertiary structure of AHL-lactonase

Biochem Biophys Res Commun. 2014 Jan 3;443(1):290-5. doi: 10.1016/j.bbrc.2013.11.101. Epub 2013 Dec 2.

Authors

P S Rajesh¹, V Ravishankar Rai²

Affiliations

¹ Department of Studies in Microbiology, University of Mysore, Manasagangotri, Mysore 570006, India.
² Department of Studies in Microbiology, University of Mysore, Manasagangotri, Mysore 570006, India. Electronic address: raivittal@gmail.com.

PMID: 24309109
DOI: 10.1016/j.bbrc.2013.11.101

Abstract

The aiiA homologous gene known to encode AHL- lactonase enzyme which hydrolyze the N-acylhomoserine lactone (AHL) quorum sensing signaling molecules produced by Gram negative bacteria. In this study, the degradation of AHL molecules was determined by cell-free lysate of endophytic Enterobacter species. The percentage of quorum quenching was confirmed and quantified by HPLC method (p<0.0001). Amplification and sequence BLAST analysis showed the presence of aiiA homologous gene in endophytic Enterobacter asburiae VT65, Enterobacter aerogenes VT66 and Enterobacter ludwigii VT70 strains. Sequence alignment analysis revealed the presence of two zinc binding sites, "HXHXDH" motif as well as tyrosine residue at the position 194. Based on known template available at Swiss-Model, putative tertiary structure of AHL-lactonase was constructed. The result showed that novel endophytic strains of Enterobacter genera encode the novel aiiA homologous gene and its structural importance for future study.

Keywords: AHL-lactonase; Enterobacter species; Quorum quenching; Tertiary structure; aiiA gene.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Carboxylic Ester Hydrolases / chemistry*
Carboxylic Ester Hydrolases / classification
Carboxylic Ester Hydrolases / genetics*
Computer Simulation
Enterobacter / enzymology*
Enterobacter / genetics*
Genes, Bacterial*
Genetic Association Studies
Metalloendopeptidases / chemistry*
Metalloendopeptidases / classification
Metalloendopeptidases / genetics*
Molecular Sequence Data
Phylogeny
Protein Structure, Tertiary
Sequence Alignment

Substances

Carboxylic Ester Hydrolases
N-acyl homoserine lactonase
Metalloendopeptidases