Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control. Issue 4 (3rd April 2019)

• Record Type: Journal Article
• Authors: Yoshitani, Kohei; Ishii, Eiji; Taniguchi, Katsuhide; Sugimoto, Hiroshi; Shiro, Yoshitsugu; Akiyama, Yoshinori; Kato, Akinori; Utsumi, Ryutaro; Eguchi, Yoko
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 83:Issue 4(2019)
• Page Start: 684
• Page End: 694
• Publication Date: 2019-04-03
• Subjects: Two-component signal transduction -- PhoQ -- EvgS -- SafA -- PDC sensor fold; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2018.1562879
• Languages: English
• ISSNs: 0916-8451

Abstract

ABSTRACT: The PhoQ/PhoP two-component signal transduction system is conserved in various Gram-negative bacteria and is often involved in the expression of virulence in pathogens. The small inner membrane protein SafA activates PhoQ in Escherichia coli independently from other known signals that control PhoQ activity. We have previously shown that SafA directly interacts with the sensor domain of the periplasmic region of PhoQ (PhoQ-SD) for activation, and that a D179R mutation in PhoQ-SD attenuates PhoQ activation by SafA. In this study, structural comparison of wild-type PhoQ-SD and D179R revealed a difference in the cavity (SD (sensory domain) pocket) found in the central core of this domain. This was the only structural difference between the two proteins. Site-directed mutagenesis of the residues surrounding the SD pocket has supported the SD pocket as a site involved in PhoQ activity. Furthermore, the SD pocket has also been shown to be involved in SafA-mediated PhoQ control. Graphical abstract: : Residues surrounding the SD pocket that affect SafA-mediated PhoQ activation