Lux-operon of the marine psychrophilic bacterium Aliivibrio logei: a comparative analysis of the LuxR1/LuxR2 regulatory activity in Escherichia coli cells
Khrulnova, Svetlana A. and Baranova, Ancha and Bazhenov, Sergey V. and Goryanin, Ignatiy I. and Konopleva, Maria N. and Maryshev, Ivan V. and Salykhova, Albina I. and Vasilyeva, Alexandra V. and Manukhov, Ilya V. and Zavilgelsky, Gennadii B.,, 162, 717-724 (2016),
doi = https://doi.org/10.1099/mic.0.000253,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= The lux-operon of the psychrophilic bioluminescent bacterium Aliivibrio logei is regulated by quorum sensing (QS). The key components of this system are LuxI, which catalyses synthesis of the autoinducer (AI), and LuxR, which activates transcription of the entire lux-operon. The lux-operon of A. logei contains two copies of the luxR gene: luxR1 and luxR2. In the present study, lux-operon sequence analysis from 16 strains of A. logei, isolated from cold habitats of the White, Baltic, Okhotsk and Bering seas, was carried out. Phylogenetic analysis showed that all isolated strains of A. logei have both copies of luxR genes which are homologous to luxR genes of the related Aliivibrio salmonicida. Evaluation of LuxR1 and LuxR2 activity showed that LuxR2 remains active at significantly lower concentrations of AI (10− 9 M) than LuxR1, which is active only at high AI concentrations (10− 6 M). As the QS response is already prominent at AI concentrations as low as 10− 8 to 10− 9 M, we conclude that LuxR2 is the main activator of the lux-operon of A. logei. The thermolabilities of LuxR1 and LuxR2 are similar and exceed that of LuxR of the mesophilic bacterium Aliivibrio fischeri. In contrast to LuxR2, LuxR1 is not a substrate of Lon protease and does not require the chaperonin GroEL/ES for its folding. This study expands our current understanding of QS regulation in A. logei as it implies differential regulation by LuxR1 and LuxR2 proteins.,
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