AidP, a novel N-Acyl homoserine lactonase gene from Antarctic Planococcus sp.

See-Too, W.S. and Ee, R. and Lim, Y.L. and Convey, P. and Pearce, D.A. and Yin, Wai Fong and Chan, Kok Gan (2017) AidP, a novel N-Acyl homoserine lactonase gene from Antarctic Planococcus sp. Scientific Reports, 7 (1). p. 42968. ISSN 2045-2322, DOI https://doi.org/10.1038/srep42968.

Preview

PDF (Full Text) AidP,_a_novel_N-acyl_homoserine_lactonase_gene_from_Antarctic_Planococcus_sp..pdf Download (1MB)

Abstract

Planococcus is a Gram-positive halotolerant bacterial genus in the phylum Firmicutes, commonly found in various habitats in Antarctica. Quorum quenching (QQ) is the disruption of bacterial cell-to-cell communication (known as quorum sensing), which has previously been described in mesophilic bacteria. This study demonstrated the QQ activity of a psychrotolerant strain, Planococcus versutus strain L10.15T, isolated from a soil sample obtained near an elephant seal wallow in Antarctica. Whole genome analysis of this bacterial strain revealed the presence of an N-acyl homoserine lactonase, an enzyme that hydrolyzes the ester bond of the homoserine lactone of N-acyl homoserine lactone (AHLs). Heterologous gene expression in E. coli confirmed its functions for hydrolysis of AHLs, and the gene was designated as aidP (autoinducer degrading gene from Planococcus sp.). The low temperature activity of this enzyme suggested that it is a novel and uncharacterized class of AHL lactonase. This study is the first report on QQ activity of bacteria isolated from the polar regions.

Item Type:	Article
Funders:	University of Malaya (UM) High Impact Research Grants (UM-MOHE HIR Grant UM.C/625/1/HIR/MOHE/CHAN/14/1, Grant No. H-50001-A000027, UM-MOHE HIR Grant UM.C/625/1/HIR/MOHE/CHAN/01, Grant No. A-000001-50001), University of Malaya: PPP grant (PG084-2015B); PPP grant (PG133-2016A)
Uncontrolled Keywords:	AidP; N-acyl homoserine lactonase; Gene; Antarctic Planococcus sp.
Subjects:	Q Science > Q Science (General) Q Science > QH Natural history
Divisions:	Faculty of Science
Depositing User:	Ms. Juhaida Abd Rahim
Date Deposited:	30 Aug 2018 04:10
Last Modified:	23 Dec 2019 06:20
URI:	http://eprints.um.edu.my/id/eprint/19033

Actions (login required)

View Item