Identification of a GntR family regulator BusRTha and its regulatory mechanism in the glycine betaine ABC transport system of Tetragenococcus halophilus
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Glycine betaine is one of the most effective compatible solutes of the halophilic lactic acid bacterium Tetragenococcus halophilus, the transportation of which is essential for its survival under salinity stress condition. In the current study, we attempted to define a glycine betaine ABC transporter system of T. halophilus, busATha, which plays an important role in adapting to salinity condition. The expression of busATha enhanced the growth of the recombinant strain under high salinity. BusRTha, a transcription regulator that represses the expression of busATha, was characterized, and the repression was abrogated under high salinity. The binding of the regulator was demonstrated through electrophoretic mobility shift assays, and the binding sites were characterized as 5′-AAA(T/G)TGAC(C/A)(G/A)T(C/A)C-3′. This is the first studied transcription regulator of T. halophilus, and our findings provide insights into the molecular mechanism of halophilic life and tools for further application of halophiles as chassis in industrial biotechnology.
KeywordsTetragenococcus halophilus Glycine betaine ABC transport system GntR family transcription regulators BusR
This work was supported by the National Natural Science Foundation of China (Grant nos. 31771962, 31271924).
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Conflict of interest
The authors declare no conflict of interest.
- Bouvier J, Bordes P, Romeo Y, Fourçans A, Bouvier I, Gutierrez C (2000) Characterization of OpuA, a glycine-betaine uptake system of Lactococcus lactis. J Mol Microbiol Biotechnol 2:199–205Google Scholar
- Man JCD, Rogosa M, Sharpe ME (1960) A medium for the cultivation of lactobacilli. J Appl Microbiol 23:130–135Google Scholar
- Obis D, Guillot A, Gripon J-C, Renault P, Bolotin A, Mistou M-Y (1999) Genetic and biochemical characterization of a high-affinity betaine uptake system (BusA) in Lactococcus lactis reveals a new functional organization within bacterial ABC transporters. J Bacteriol 181:6238–6246Google Scholar
- Rigali S, Schlicht M, Hoskisson P, Nothaft H, Merzbacher M, Joris B, Titgemeyer F (2004) Extending the classification of bacterial transcription factors beyond the helix-turn-helix motif as an alternative approach to discover new cis/trans relationships. Nucleic Acids Res 32:3418–3426CrossRefGoogle Scholar