Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control
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 a...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2019-04, Vol.83 (4), p.684-694 |
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| container_title | Bioscience, biotechnology, and biochemistry |
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| creator | Yoshitani, Kohei Ishii, Eiji Taniguchi, Katsuhide Sugimoto, Hiroshi Shiro, Yoshitsugu Akiyama, Yoshinori Kato, Akinori Utsumi, Ryutaro Eguchi, Yoko |
| description | 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.
Residues surrounding the SD pocket that affect SafA-mediated PhoQ activation |
| doi_str_mv | 10.1080/09168451.2018.1562879 |
| format | Article |
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Residues surrounding the SD pocket that affect SafA-mediated PhoQ activation</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2018.1562879</identifier><identifier>PMID: 30632929</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>EvgS ; PDC sensor fold ; PhoQ ; SafA ; Two-component signal transduction</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2019-04, Vol.83 (4), p.684-694</ispartof><rights>2018 Informa UK Limited, trading as Taylor & Francis Group 2018</rights><rights>2019 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-80a4c8c2204536913571d4414eea3df4cc0a3bfe315c5540febfb58ca42833573</citedby><cites>FETCH-LOGICAL-c544t-80a4c8c2204536913571d4414eea3df4cc0a3bfe315c5540febfb58ca42833573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30632929$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshitani, Kohei</creatorcontrib><creatorcontrib>Ishii, Eiji</creatorcontrib><creatorcontrib>Taniguchi, Katsuhide</creatorcontrib><creatorcontrib>Sugimoto, Hiroshi</creatorcontrib><creatorcontrib>Shiro, Yoshitsugu</creatorcontrib><creatorcontrib>Akiyama, Yoshinori</creatorcontrib><creatorcontrib>Kato, Akinori</creatorcontrib><creatorcontrib>Utsumi, Ryutaro</creatorcontrib><creatorcontrib>Eguchi, Yoko</creatorcontrib><title>Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>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.
Residues surrounding the SD pocket that affect SafA-mediated PhoQ activation</description><subject>EvgS</subject><subject>PDC sensor fold</subject><subject>PhoQ</subject><subject>SafA</subject><subject>Two-component signal transduction</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNqNkN1OwyAYhonRuDm9BA030AkF-nPmsvizZIka9bj5SiFj6WChTLO7l67TQ-MR8OZ535AHoWtKppQU5JaUNCu4oNOU0GJKRZYWeXmCxpTxPMlKnp-icc8kPTRCF123JiQGgp6jESMZS8u0HKP1olE2GG0kBOMsdhqDxcYG5S20WMKnCfv4xmGl8MvKveJO2c553LgNxFjH6yEGGcyBBdvgN9CzZKMaA0E1WDobvGsv0ZmGtlNXx3OCPh7u3-dPyfL5cTGfLRMpOA9JQYDLQqYp4YJlJWUipw3nlCsFrNFcSgKs1opRIYXgRKta16KQwNOCRZhNkBh2pXdd55Wutt5swO8rSqreXfXjrurdVUd3sXcz9La7Ov79t_UjKwJkANxu--_Nu6FibDS1gS_n26YKsG-d1x6sNF3F_p74BlUljCw</recordid><startdate>20190403</startdate><enddate>20190403</enddate><creator>Yoshitani, Kohei</creator><creator>Ishii, Eiji</creator><creator>Taniguchi, Katsuhide</creator><creator>Sugimoto, Hiroshi</creator><creator>Shiro, Yoshitsugu</creator><creator>Akiyama, Yoshinori</creator><creator>Kato, Akinori</creator><creator>Utsumi, Ryutaro</creator><creator>Eguchi, Yoko</creator><general>Taylor & Francis</general><general>Oxford University Press</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20190403</creationdate><title>Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control</title><author>Yoshitani, Kohei ; Ishii, Eiji ; Taniguchi, Katsuhide ; Sugimoto, Hiroshi ; Shiro, Yoshitsugu ; Akiyama, Yoshinori ; Kato, Akinori ; Utsumi, Ryutaro ; Eguchi, Yoko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-80a4c8c2204536913571d4414eea3df4cc0a3bfe315c5540febfb58ca42833573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>EvgS</topic><topic>PDC sensor fold</topic><topic>PhoQ</topic><topic>SafA</topic><topic>Two-component signal transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoshitani, Kohei</creatorcontrib><creatorcontrib>Ishii, Eiji</creatorcontrib><creatorcontrib>Taniguchi, Katsuhide</creatorcontrib><creatorcontrib>Sugimoto, Hiroshi</creatorcontrib><creatorcontrib>Shiro, Yoshitsugu</creatorcontrib><creatorcontrib>Akiyama, Yoshinori</creatorcontrib><creatorcontrib>Kato, Akinori</creatorcontrib><creatorcontrib>Utsumi, Ryutaro</creatorcontrib><creatorcontrib>Eguchi, Yoko</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yoshitani, Kohei</au><au>Ishii, Eiji</au><au>Taniguchi, Katsuhide</au><au>Sugimoto, Hiroshi</au><au>Shiro, Yoshitsugu</au><au>Akiyama, Yoshinori</au><au>Kato, Akinori</au><au>Utsumi, Ryutaro</au><au>Eguchi, Yoko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2019-04-03</date><risdate>2019</risdate><volume>83</volume><issue>4</issue><spage>684</spage><epage>694</epage><pages>684-694</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><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.
Residues surrounding the SD pocket that affect SafA-mediated PhoQ activation</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>30632929</pmid><doi>10.1080/09168451.2018.1562879</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2019-04, Vol.83 (4), p.684-694 |
| issn | 0916-8451 1347-6947 |
| language | eng |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles |
| subjects | EvgS PDC sensor fold PhoQ SafA Two-component signal transduction |
| title | Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control |
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