Modulation of CrbS-Dependent Activation of the Acetate Switch in Vibrio cholerae
Author(s) -
Itai Muzhingi,
Cecilia Prado,
Mariame Sylla,
Frances F. Diehl,
Duy K. Nguyen,
Mariah M. Servos,
Stephany Flores Ramos,
Alexandra E. Purdy
Publication year - 2018
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00380-18
Subject(s) - biology , vibrio cholerae , histidine kinase , signal transduction , microbiology and biotechnology , histidine , biochemistry , flux (metallurgy) , kinase , phosphorylation , bacteria , genetics , enzyme , materials science , metallurgy
CrbS is a member of a unique family of sensor histidine kinases, as its structure suggests that it may link signaling to the transport of a molecule. However, mechanisms through which CrbS senses and communicates information about the outside world are unknown. In theVibrionaceae , orthologs of CrbS regulate acetate metabolism, which can, in turn, affect interactions with host organisms. Here, we situate CrbS within a larger regulatory framework, demonstrating thatcrbS is regulated by nutrient-sensing systems. Furthermore, CrbS domains may play various roles in signaling during infection and growth in culture, suggesting a unique mechanism of host recognition. Finally, we define the roles of additional pathways in acetate flux, as a foundation for further studies of this metabolic nexus point.
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