C Terminus of the Flagellar Muramidase SltF Modulates the Interaction with FlgJ in Rhodobacter sphaeroides
Macromolecular structures such as the bacterial flagellum in Gram-negative bacteria must traverse the cell wall. Lytic transglycosylases are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. We have previously shown that in Rhodobact...
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| Veröffentlicht in: | Journal of Bacteriology 2012-09, Vol.194 (17), p.4513-4520 |
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| creator | de la Mora, Javier Osorio-Valeriano, Manuel González-Pedrajo, Bertha Ballado, Teresa Camarena, Laura Dreyfus, Georges |
| description | Macromolecular structures such as the bacterial flagellum in Gram-negative bacteria must traverse the cell wall. Lytic transglycosylases are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. We have previously shown that in Rhodobacter sphaeroides SltF, the flagellar muramidase, and FlgJ, a flagellar scaffold protein, are separate entities that interact in the periplasm. In this study we show that the export of SltF to the periplasm is dependent on the SecA pathway. A deletion analysis of the C-terminal portion of SltF shows that this region is required for SltF-SltF interaction. These C terminus-truncated mutants lose the capacity to interact with themselves and also bind FlgJ with higher affinity than does the wild-type protein. We propose that this region modulates the interaction with the scaffold protein FlgJ during the assembly process. |
| doi_str_mv | 10.1128/JB.00460-12 |
| format | Article |
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Lytic transglycosylases are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. We have previously shown that in Rhodobacter sphaeroides SltF, the flagellar muramidase, and FlgJ, a flagellar scaffold protein, are separate entities that interact in the periplasm. In this study we show that the export of SltF to the periplasm is dependent on the SecA pathway. A deletion analysis of the C-terminal portion of SltF shows that this region is required for SltF-SltF interaction. These C terminus-truncated mutants lose the capacity to interact with themselves and also bind FlgJ with higher affinity than does the wild-type protein. We propose that this region modulates the interaction with the scaffold protein FlgJ during the assembly process.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/JB.00460-12</identifier><identifier>PMID: 22707709</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Adenosine Triphosphatases - metabolism ; Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacteriology ; Cell Wall - metabolism ; cell walls ; Flagella - enzymology ; flagellum ; Gram-negative bacteria ; lysozyme ; Membrane Transport Proteins - metabolism ; Molecular Sequence Data ; Muramidase - chemistry ; Muramidase - metabolism ; mutants ; Mutation ; Peptides ; Peptidoglycan Glycosyltransferase - metabolism ; peptidoglycans ; Proteins ; Rhodobacter sphaeroides ; Rhodobacter sphaeroides - metabolism ; SEC Translocation Channels ; Sequence Alignment ; Sequence Deletion</subject><ispartof>Journal of Bacteriology, 2012-09, Vol.194 (17), p.4513-4520</ispartof><rights>Copyright American Society for Microbiology Sep 2012</rights><rights>Copyright © 2012, American Society for Microbiology. All Rights Reserved. 2012 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-4f968d21d7c1f429d2b254f971ae87ea255d5e83d80f2f80886874179fc913963</citedby><cites>FETCH-LOGICAL-c493t-4f968d21d7c1f429d2b254f971ae87ea255d5e83d80f2f80886874179fc913963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3415505/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3415505/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22707709$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de la Mora, Javier</creatorcontrib><creatorcontrib>Osorio-Valeriano, Manuel</creatorcontrib><creatorcontrib>González-Pedrajo, Bertha</creatorcontrib><creatorcontrib>Ballado, Teresa</creatorcontrib><creatorcontrib>Camarena, Laura</creatorcontrib><creatorcontrib>Dreyfus, Georges</creatorcontrib><title>C Terminus of the Flagellar Muramidase SltF Modulates the Interaction with FlgJ in Rhodobacter sphaeroides</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>Macromolecular structures such as the bacterial flagellum in Gram-negative bacteria must traverse the cell wall. Lytic transglycosylases are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. We have previously shown that in Rhodobacter sphaeroides SltF, the flagellar muramidase, and FlgJ, a flagellar scaffold protein, are separate entities that interact in the periplasm. In this study we show that the export of SltF to the periplasm is dependent on the SecA pathway. A deletion analysis of the C-terminal portion of SltF shows that this region is required for SltF-SltF interaction. These C terminus-truncated mutants lose the capacity to interact with themselves and also bind FlgJ with higher affinity than does the wild-type protein. We propose that this region modulates the interaction with the scaffold protein FlgJ during the assembly process.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Cell Wall - metabolism</subject><subject>cell walls</subject><subject>Flagella - enzymology</subject><subject>flagellum</subject><subject>Gram-negative bacteria</subject><subject>lysozyme</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>mutants</subject><subject>Mutation</subject><subject>Peptides</subject><subject>Peptidoglycan Glycosyltransferase - metabolism</subject><subject>peptidoglycans</subject><subject>Proteins</subject><subject>Rhodobacter sphaeroides</subject><subject>Rhodobacter sphaeroides - metabolism</subject><subject>SEC Translocation Channels</subject><subject>Sequence Alignment</subject><subject>Sequence Deletion</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpd0s1v0zAUAHALgVg3OHEHCy5IKMPPH7F9QWIVhVWbkNh2ttzESVwlcbETpv33uOuYgJMlv5-f3ocRegXkFICqj-uzU0J4SQqgT9ACiFaFEIw8RQtCKBQaNDtCxyltCQHOBX2OjiiVREqiF2i7xNcuDn6cEw4NnjqHV71tXd_biC_naAdf2-TwVT-t8GWo595OLt2783Fy0VaTDyO-9VOXH7Zr7Ef8owt12OSIizjtOuti8LVLL9CzxvbJvXw4T9DN6sv18ltx8f3r-fLzRVFxzaaCN7pUNYVaVtBwqmu6oSJfSrBOSWepELVwitWKNLRRRKlSSQ5SN5UGpkt2gj4d8u7mzeDqyo1TtL3ZRT_YeGeC9ebfyOg704ZfhnEQgoic4P1Dghh-zi5NZvCp2o9kdGFOBkqpBC05J5m--49uwxzH3J4BwhhXZW4mqw8HVcWQUnTNYzFAzH6HZn1m7ndogGb9-u_6H-2fpWXw9gA633a3Pjpj02C2GwOaG5CGC2AZvTmgxgZj2-iTubmiBMT-F2iiNPsND3uqrQ</recordid><startdate>20120901</startdate><enddate>20120901</enddate><creator>de la Mora, Javier</creator><creator>Osorio-Valeriano, Manuel</creator><creator>González-Pedrajo, Bertha</creator><creator>Ballado, Teresa</creator><creator>Camarena, Laura</creator><creator>Dreyfus, Georges</creator><general>American Society for Microbiology</general><scope>FBQ</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>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20120901</creationdate><title>C Terminus of the Flagellar Muramidase SltF Modulates the Interaction with FlgJ in Rhodobacter sphaeroides</title><author>de la Mora, Javier ; 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| issn | 0021-9193 1098-5530 1067-8832 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Adenosine Triphosphatases - metabolism Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteriology Cell Wall - metabolism cell walls Flagella - enzymology flagellum Gram-negative bacteria lysozyme Membrane Transport Proteins - metabolism Molecular Sequence Data Muramidase - chemistry Muramidase - metabolism mutants Mutation Peptides Peptidoglycan Glycosyltransferase - metabolism peptidoglycans Proteins Rhodobacter sphaeroides Rhodobacter sphaeroides - metabolism SEC Translocation Channels Sequence Alignment Sequence Deletion |
| title | C Terminus of the Flagellar Muramidase SltF Modulates the Interaction with FlgJ in Rhodobacter sphaeroides |
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