Lau, Yin Yin and How, Kah Yan and Yin, Wai Fong and Chan, Kok Gan (2018) Cloning and characterization of short‐chain N ‐acyl homoserine lactone‐producing Enterobacter asburiae strain L1 from lettuce leaves. MicrobiologyOpen, 7 (6). e00610. ISSN 2045-8827, DOI https://doi.org/10.1002/mbo3.610.
Full text not available from this repository.Abstract
In gram-negative bacteria, bacterial communication or quorum sensing (QS) is achieved using common signaling molecules known as N-acyl homoserine lactones (AHL). We have previously reported the genome of AHL-producing bacterium, Enterobacter asburiae strain L1. In silico analysis of the strain L1 genome revealed the presence of a pair of luxI/R genes responsible for AHL-type QS, designated as easIR. In this work, the 639 bp luxI homolog, encoding 212 amino acids, have been cloned and overexpressed in Escherichia coli BL21 (DE3)pLysS. The purified protein (~25 kDa) shares high similarity to several members of the LuxI family among different E asburiae strains. Our findings showed that the heterologously expressed EasI protein has activated violacein production by AHL biosensor Chromobacterium violaceum CV026 as the wild-type E. asburiae. The mass spectrometry analysis showed the production of N-butanoyl homoserine lactone and N–hexanoyl homoserine lactone from induced E. coli harboring the recombinant EasI, suggesting that EasI is a functional AHL synthase. E. asburiae strain L1 was also shown to possess biofilm-forming characteristic activity using crystal violet binding assay. This is the first report on cloning and characterization of the luxI homolog from E. asburiae.
Item Type: | Article |
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Funders: | University of Malaya for Research Grant (GA001-2016, GA002-2016), University of Malaya for the PPP Grant PG086-2015B |
Uncontrolled Keywords: | AHL synthase; biofilm; Enterobacter asburiae; N-acyl homoserine lactone; protein expression; quorum sensing |
Subjects: | Q Science > Q Science (General) Q Science > QH Natural history |
Divisions: | Faculty of Science > Institute of Biological Sciences |
Depositing User: | Ms. Juhaida Abd Rahim |
Date Deposited: | 26 Jun 2019 04:39 |
Last Modified: | 26 Jun 2019 04:39 |
URI: | http://eprints.um.edu.my/id/eprint/21544 |
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