Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus
Precise regulation of the number and placement of flagella is critical for the mono-flagellated bacterium Vibrio alginolyticus to swim efficiently. We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2009-11, Vol.146 (5), p.643-650 |
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| creator | Kusumoto, Akiko Nishioka, Noriko Kojima, Seiji Homma, Michio |
| description | Precise regulation of the number and placement of flagella is critical for the mono-flagellated bacterium Vibrio alginolyticus to swim efficiently. We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG interacts with FlhF to prevent FlhF from localizing to the pole, and thus FlhG negatively regulates the flagellar number in V. alginolyticus cells. To investigate the role of the GTP-binding motif of FlhF, we generated a series of alanine-replacement mutations at the positions that are highly conserved among homologous proteins. The results indicate that there is a correlation between the polar localization and the ability to produce flagella in the mutants. We investigated whether the mutations in the GTP-binding motif affected the ability to interact with FlhG. In contrast to our prediction, no significant difference was detected in the interaction with FlhG between the wild-type and mutant FlhFs. We showed that the GTP-binding motif of FlhF is important for polar localization of the flagellum but not for the interaction with FlhG. |
| doi_str_mv | 10.1093/jb/mvp109 |
| format | Article |
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We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG interacts with FlhF to prevent FlhF from localizing to the pole, and thus FlhG negatively regulates the flagellar number in V. alginolyticus cells. To investigate the role of the GTP-binding motif of FlhF, we generated a series of alanine-replacement mutations at the positions that are highly conserved among homologous proteins. The results indicate that there is a correlation between the polar localization and the ability to produce flagella in the mutants. We investigated whether the mutations in the GTP-binding motif affected the ability to interact with FlhG. In contrast to our prediction, no significant difference was detected in the interaction with FlhG between the wild-type and mutant FlhFs. We showed that the GTP-binding motif of FlhF is important for polar localization of the flagellum but not for the interaction with FlhG.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvp109</identifier><identifier>PMID: 19605463</identifier><language>eng</language><publisher>England: Japanese Biochemical Society</publisher><subject>Alanine - metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; bacterial flagella ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Cell Polarity ; DNA Mutational Analysis ; Flagella - metabolism ; Green Fluorescent Proteins - metabolism ; GTP-binding motif ; Guanosine Triphosphate - metabolism ; Immunoprecipitation ; Molecular Sequence Data ; Monomeric GTP-Binding Proteins - chemistry ; Monomeric GTP-Binding Proteins - metabolism ; Movement ; Mutant Proteins - chemistry ; Mutant Proteins - metabolism ; Mutation - genetics ; Plasmids - genetics ; polar flagellum ; Protein Binding ; Protein Transport ; Recombinant Fusion Proteins - metabolism ; Vibrio alginolyticus - cytology ; Vibrio alginolyticus - metabolism</subject><ispartof>Journal of biochemistry (Tokyo), 2009-11, Vol.146 (5), p.643-650</ispartof><rights>The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-ad889f3ea6ac9abae60d2dce291b28575bd563188252a9c62bea522abe8f336c3</citedby><cites>FETCH-LOGICAL-c467t-ad889f3ea6ac9abae60d2dce291b28575bd563188252a9c62bea522abe8f336c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1584,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19605463$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kusumoto, Akiko</creatorcontrib><creatorcontrib>Nishioka, Noriko</creatorcontrib><creatorcontrib>Kojima, Seiji</creatorcontrib><creatorcontrib>Homma, Michio</creatorcontrib><title>Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Precise regulation of the number and placement of flagella is critical for the mono-flagellated bacterium Vibrio alginolyticus to swim efficiently. We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG interacts with FlhF to prevent FlhF from localizing to the pole, and thus FlhG negatively regulates the flagellar number in V. alginolyticus cells. To investigate the role of the GTP-binding motif of FlhF, we generated a series of alanine-replacement mutations at the positions that are highly conserved among homologous proteins. The results indicate that there is a correlation between the polar localization and the ability to produce flagella in the mutants. We investigated whether the mutations in the GTP-binding motif affected the ability to interact with FlhG. In contrast to our prediction, no significant difference was detected in the interaction with FlhG between the wild-type and mutant FlhFs. We showed that the GTP-binding motif of FlhF is important for polar localization of the flagellum but not for the interaction with FlhG.</description><subject>Alanine - metabolism</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>bacterial flagella</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Cell Polarity</subject><subject>DNA Mutational Analysis</subject><subject>Flagella - metabolism</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>GTP-binding motif</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Immunoprecipitation</subject><subject>Molecular Sequence Data</subject><subject>Monomeric GTP-Binding Proteins - chemistry</subject><subject>Monomeric GTP-Binding Proteins - metabolism</subject><subject>Movement</subject><subject>Mutant Proteins - chemistry</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation - genetics</subject><subject>Plasmids - genetics</subject><subject>polar flagellum</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Vibrio alginolyticus - cytology</subject><subject>Vibrio alginolyticus - metabolism</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90EGP1CAYBmBiNO64evAPKAcT46FugULb42Z0dk12daK7OvFCPiidYaRlBKrOf_BH27Gj3rwAX3h4Q16EHpP8JclrdrZVZ9233Xi8g2ak5CKjgpO7aJbnlGQ1LVYn6EGM28NIGbuPTkgtcl4INkM_r4cEyfoeHD4fl320EfsWp43BFzfLTNm-sf0aX_tk28PFwm0W-PvG6g1-b9aDg2Tib_126JQJGPoGLx1o05k-_UlaegdhfApr49zQYdvjj1YF6zG4te292yerh_gQ3WvBRfPouJ-i28Xrm_lldvXu4s38_CrThShTBk1V1S0zIEDXoMCIvKGNNrQmila85KrhgpGqopxCrQVVBjiloEzVMiY0O0XPp9xd8F8HE5PsbNTj16A3foiyZAWhRVnwUb6YpA4-xmBauQu2g7CXJJeH7uVWyan70T45pg6qM80_eSx7BM8m4Ifdf3OyidmYzI-_EMIXKUpWcnm5-izpquLV_NMrOR_908m34CWsg43y9gPNCcuJqCtSMvYLFgWmOg</recordid><startdate>20091101</startdate><enddate>20091101</enddate><creator>Kusumoto, Akiko</creator><creator>Nishioka, Noriko</creator><creator>Kojima, Seiji</creator><creator>Homma, Michio</creator><general>Japanese Biochemical Society</general><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20091101</creationdate><title>Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus</title><author>Kusumoto, Akiko ; Nishioka, Noriko ; Kojima, Seiji ; Homma, Michio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c467t-ad889f3ea6ac9abae60d2dce291b28575bd563188252a9c62bea522abe8f336c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Alanine - metabolism</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>bacterial flagella</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Cell Polarity</topic><topic>DNA Mutational Analysis</topic><topic>Flagella - metabolism</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>GTP-binding motif</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Immunoprecipitation</topic><topic>Molecular Sequence Data</topic><topic>Monomeric GTP-Binding Proteins - chemistry</topic><topic>Monomeric GTP-Binding Proteins - metabolism</topic><topic>Movement</topic><topic>Mutant Proteins - chemistry</topic><topic>Mutant Proteins - metabolism</topic><topic>Mutation - genetics</topic><topic>Plasmids - genetics</topic><topic>polar flagellum</topic><topic>Protein Binding</topic><topic>Protein Transport</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Vibrio alginolyticus - cytology</topic><topic>Vibrio alginolyticus - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kusumoto, Akiko</creatorcontrib><creatorcontrib>Nishioka, Noriko</creatorcontrib><creatorcontrib>Kojima, Seiji</creatorcontrib><creatorcontrib>Homma, Michio</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kusumoto, Akiko</au><au>Nishioka, Noriko</au><au>Kojima, Seiji</au><au>Homma, Michio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2009-11-01</date><risdate>2009</risdate><volume>146</volume><issue>5</issue><spage>643</spage><epage>650</epage><pages>643-650</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Precise regulation of the number and placement of flagella is critical for the mono-flagellated bacterium Vibrio alginolyticus to swim efficiently. We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG interacts with FlhF to prevent FlhF from localizing to the pole, and thus FlhG negatively regulates the flagellar number in V. alginolyticus cells. To investigate the role of the GTP-binding motif of FlhF, we generated a series of alanine-replacement mutations at the positions that are highly conserved among homologous proteins. The results indicate that there is a correlation between the polar localization and the ability to produce flagella in the mutants. We investigated whether the mutations in the GTP-binding motif affected the ability to interact with FlhG. In contrast to our prediction, no significant difference was detected in the interaction with FlhG between the wild-type and mutant FlhFs. We showed that the GTP-binding motif of FlhF is important for polar localization of the flagellum but not for the interaction with FlhG.</abstract><cop>England</cop><pub>Japanese Biochemical Society</pub><pmid>19605463</pmid><doi>10.1093/jb/mvp109</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Alanine - metabolism Amino Acid Motifs Amino Acid Sequence bacterial flagella Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cell Polarity DNA Mutational Analysis Flagella - metabolism Green Fluorescent Proteins - metabolism GTP-binding motif Guanosine Triphosphate - metabolism Immunoprecipitation Molecular Sequence Data Monomeric GTP-Binding Proteins - chemistry Monomeric GTP-Binding Proteins - metabolism Movement Mutant Proteins - chemistry Mutant Proteins - metabolism Mutation - genetics Plasmids - genetics polar flagellum Protein Binding Protein Transport Recombinant Fusion Proteins - metabolism Vibrio alginolyticus - cytology Vibrio alginolyticus - metabolism |
| title | Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus |
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