The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis
Erp (exported repetitive protein), also known as P36, Pirg and Rv3810, is a member of a mycobacteria-specific family of extracellular proteins. In pathogenic species, the erp gene has been described as a virulence factor. The Erp proteins comprise three domains. The N- and C-terminal domains are sim...
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| Veröffentlicht in: | FEMS microbiology letters 2004-02, Vol.231 (2), p.191-196 |
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| container_title | FEMS microbiology letters |
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| creator | Kocíncová, Dana Sondén, Berit Leila de Mendonça-Lima Gicquel, Brigitte Jean-Marc Reyrat |
| description | Erp (exported repetitive protein), also known as P36, Pirg and Rv3810, is a member of a mycobacteria-specific family of extracellular proteins. In pathogenic species, the erp gene has been described as a virulence factor. The Erp proteins comprise three domains. The N- and C-terminal domains are similar in all mycobacterial species, while the central domain consists of a repeated module that differs considerably between species. Here we show that the Erp protein is loosely attached to the surface and that the carboxy-terminal domain, which displays hydrophobic features, anchors Erp at the surface of the bacillus. The hydrophobic region is not necessary for the complementation of the altered colony morphology of a Mycobacterium smegmatis erp− mutant but proved to be necessary to achieve resistance to detergent at wild-type levels. |
| doi_str_mv | 10.1016/S0378-10970300964-9 |
| format | Article |
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The hydrophobic region is not necessary for the complementation of the altered colony morphology of a Mycobacterium smegmatis erp− mutant but proved to be necessary to achieve resistance to detergent at wild-type levels.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/S0378-10970300964-9</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Complementation ; Erp protein ; Hydrophobicity ; Microbiology ; Morphology ; Mycobacterium smegmatis ; Proteins ; Species ; Virulence ; Virulence factors</subject><ispartof>FEMS microbiology letters, 2004-02, Vol.231 (2), p.191-196</ispartof><rights>2004 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids></links><search><creatorcontrib>Kocíncová, Dana</creatorcontrib><creatorcontrib>Sondén, Berit</creatorcontrib><creatorcontrib>Leila de Mendonça-Lima</creatorcontrib><creatorcontrib>Gicquel, Brigitte</creatorcontrib><creatorcontrib>Jean-Marc Reyrat</creatorcontrib><title>The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis</title><title>FEMS microbiology letters</title><description>Erp (exported repetitive protein), also known as P36, Pirg and Rv3810, is a member of a mycobacteria-specific family of extracellular proteins. 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The hydrophobic region is not necessary for the complementation of the altered colony morphology of a Mycobacterium smegmatis erp− mutant but proved to be necessary to achieve resistance to detergent at wild-type levels.</description><subject>Complementation</subject><subject>Erp protein</subject><subject>Hydrophobicity</subject><subject>Microbiology</subject><subject>Morphology</subject><subject>Mycobacterium smegmatis</subject><subject>Proteins</subject><subject>Species</subject><subject>Virulence</subject><subject>Virulence factors</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNjrtOxDAQRS0EEsvjC2hGog5MNu8aLaKh2u1XE8chXtlxGNuCfAm_i5EQNdUt7tG5V4i7HB9yzOvHPRZNm-XYNVggdnWZdWdik1dNmdVd3Z6LzR9wKa68PyFiucV6I74Ok4IdL7CwC0rPoD3QLCfHagAKEFLtI48kFfQrEEji3n2uWVBs9UwGpnVgt0yu1xIGZyk5aB5-PNoujgPNAUbHIJUx2QcZAz5wlCGygsS-rtL1JJNORwveqjdLQfsbcTGS8er2N6_F_fPu8PSSpZ_vUflwPLnIad8ftwV2RVuVVVP8j_oGZf5gxA</recordid><startdate>20040201</startdate><enddate>20040201</enddate><creator>Kocíncová, Dana</creator><creator>Sondén, Berit</creator><creator>Leila de Mendonça-Lima</creator><creator>Gicquel, Brigitte</creator><creator>Jean-Marc Reyrat</creator><general>Oxford University Press</general><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20040201</creationdate><title>The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis</title><author>Kocíncová, Dana ; 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| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2004-02, Vol.231 (2), p.191-196 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_journals_2309385457 |
| source | Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Complementation Erp protein Hydrophobicity Microbiology Morphology Mycobacterium smegmatis Proteins Species Virulence Virulence factors |
| title | The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis |
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