Abstract
Because of ubiquity of thioesters, thioesterases play a critical role in metabolism, membrane biosynthesis, signal transduction, and gene regulation. In many bacteria, YbgC is such an enzyme, whose coding gene mostly resides in the tol-pal cluster. Although all other proteins encoded in the tol-pal cluster are clearly involved in maintaining cell envelope integrity and cell division, little is known about the physiological role of YbgC. In this study, we identify in Shewanella oneidensis, a γ-proteobacterium used as a research model for environmental microbes, YbgC as a motility regulator. The loss of YbgC results in enhanced motility, which is likely due to the increased rotation rate of the flagellum. The regulatory function of YbgC requires its thioesterase activity but could not be replaced by YbgC homologues of other bacteria. We further show that the regulation of YbgC is mediated by the second message c-di-GMP.
Highlights
Gram-negative bacteria are characterized by the presence of an inner membrane (IM) and a distinct outer membrane (OM), separated by a semi-aqueous compartment termed the periplasm where the peptidoglycan (PG) layer resides[1]
As thioesters are widely found in a variety of metabolites from numerous biological processes, thioesterases play a critical role in metabolism, membrane biosynthesis, signal transduction, and gene regulation[16]
A recent report about the E. coli Tol-Pal system has revealed that YbgF coordinates envelope machines facilitating septal PG synthesis and OM constriction (Tol system), leaving YbgC the only protein encoded in the tol-pal cluster without a clearly defined role[12]
Summary
Gram-negative bacteria are characterized by the presence of an inner membrane (IM) and a distinct outer membrane (OM), separated by a semi-aqueous compartment termed the periplasm where the peptidoglycan (PG) layer resides[1]. These structures all together constitute the cell envelope, which is essential for survival and proliferation in environments. Integrity and function of the cell envelope in part relies on membrane-associated protein complexes that transport substrate and energy between the environment and the cytoplasm[2,3,4]. Mechanisms underlying polar localization of FlhF and the flagellum, remain unknown
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