Figure 8: Working model for the role of Hfq in the regulation of adhesins in Y. enterocolitica. | Scientific Reports

Figure 8: Working model for the role of Hfq in the regulation of adhesins in Y. enterocolitica.

From: The RNA Chaperone Hfq Is Essential for Virulence and Modulates the Expression of Four Adhesins in Yersinia enterocolitica

Figure 8

The production of adhesins (in orange) is controlled by the RNA chaperone Hfq through its influence on transcriptional regulators (in blue) and through post-transcriptional inhibition (action on the grey arrows). We hypothesize that Hfq acts in concert with different cofactors (boxed), likely sRNAs, to exert its post-transcriptional effects on the different adhesins. Hfq represses expression of myfA (only when bacteria are grown at low pH) at the post-transcriptional level in logarithmic phase and through an effect on myfA transcription at 27 °C (in stationary phase). Production of Ail is controlled by Hfq at the post-transcriptional level at 37 °C. Hfq exerts a complex influence on YadA production, independently of VirF, the major direct transcriptional activator of yadA: (i) At 27 °C, Hfq promotes expression of yadA, possibly at the transcriptional level through its effect on the direct transcriptional repressor OmpR; (ii) conversely with the help of an unknown cofactor produced at 37 °C in stationary phase, Hfq represses yadA post-transcriptionally, (iii) ultimately, through its impact on proteases, like the periplasmic DegP, Hfq might also control YadA protein stability. Hfq controls the expression ompR and rovA which encode two of the four DNA-binding proteins that directly regulate invA. Finally, production of OmpX is negatively controlled by Hfq through its concerted effects on the transcriptional regulators RovA and OmpR and on the post-transcriptional level in coherent feed-forward loops. Black lines represent a reported direct regulation, such as the direct binding of a transcriptional regulator of the gene promoter (e.g. RovA and OmpR on the promoter region of invA) or the direct interaction of YadA with the protease DegP.

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