Identification of the YfgF MASE1 domain as a modulator of bacterial responses to aspartate

LACEY, M., AGASING, A., LOWRY, R. and GREEN, J. (2013). Identification of the YfgF MASE1 domain as a modulator of bacterial responses to aspartate. Open Biology, 3 (6), p. 130046.

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Official URL: http://dx.doi.org/10.1098/rsob.130046
Link to published version:: https://doi.org/10.1098/rsob.130046
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    Abstract

    Complex 3'-5'-cyclic diguanylic acid (c-di-GMP) responsive regulatory networks that are modulated by the action of multiple diguanylate cyclases (DGC; GGDEF domain proteins) and phosphodiesterases (PDE; EAL domain proteins) have evolved in many bacteria. YfgF proteins possess a membrane-anchoring domain (MASE1), a catalytically inactive GGDEF domain and a catalytically active EAL domain. Here, sustained expression of the Salmonella enterica spp. Enterica ser. Enteritidis YfgF protein is shown to mediate inhibition of the formation of the aspartate chemotactic ring on motility agar under aerobic conditions. This phenomenon was c-di-GMP-independent because it occurred in a Salmonella strain that lacked the ability to synthesize c-di-GMP and also when PDE activity was abolished by site-directed mutagenesis of the EAL domain. YfgF-mediated inhibition of aspartate chemotactic ring formation was impaired in the altered redox environment generated by exogenous p-benzoquinone. This ability of YfgF to inhibit the response to aspartate required a motif, (213)Lys-Lys-Glu(215), in the predicted cytoplasmic loop between trans-membrane regions 5 and 6 of the MASE1 domain. Thus, for the first time the function of a MASE1 domain as a redox-responsive regulator of bacterial responses to aspartate has been shown.

    Item Type: Article
    Research Institute, Centre or Group - Does NOT include content added after October 2018: Biomolecular Sciences Research Centre
    Identification Number: https://doi.org/10.1098/rsob.130046
    Page Range: p. 130046
    Depositing User: Users 3084 not found.
    Date Deposited: 19 Aug 2013 09:26
    Last Modified: 12 May 2018 14:11
    URI: http://shura.shu.ac.uk/id/eprint/7271

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