Role of DegP for two-partner secretion in Bordetella
Sorting of proteins destined to the surface or the extracellular milieu is mediated by specific machineries, which guide the protein substrates towards the proper route of secretion and determine the compartment in which folding occurs. In Gram-negative bacteria, the two-partner secretion (TPS) path...
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| Veröffentlicht in: | Molecular microbiology 2009-10, Vol.74 (2), p.315-329 |
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| creator | Baud, C Hodak, H Willery, E Drobecq, H Locht, C Jamin, M Jacob-Dubuisson, F |
| description | Sorting of proteins destined to the surface or the extracellular milieu is mediated by specific machineries, which guide the protein substrates towards the proper route of secretion and determine the compartment in which folding occurs. In Gram-negative bacteria, the two-partner secretion (TPS) pathway is dedicated to the secretion of large proteins rich in β-helical structure. The secretion of the filamentous haemagglutinin (FHA), a 230 kDa adhesin of Bordetella pertussis, represents a model TPS system. FHA is exported by the Sec machinery and transits through the periplasm in an extended conformation. From there it is translocated across the outer membrane by its dedicated transporter FhaC to finally fold into a long β-helix at the cell surface in a progressive manner. In this work, we show that B. pertussis lacking the periplasmic chaperone/protease DegP has a strong growth defect at 37°C, and the integrity of its outer membrane is compromised. While both phenotypes are significantly aggravated by the presence of FHA, the chaperone activity of DegP markedly alleviates the periplasmic stress. In vitro, DegP binds to non-native FHA with high affinity. We propose that DegP chaperones the extended FHA polypeptide in the periplasm and is thus involved in the TPS pathway. |
| doi_str_mv | 10.1111/j.1365-2958.2009.06860.x |
| format | Article |
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In Gram-negative bacteria, the two-partner secretion (TPS) pathway is dedicated to the secretion of large proteins rich in β-helical structure. The secretion of the filamentous haemagglutinin (FHA), a 230 kDa adhesin of Bordetella pertussis, represents a model TPS system. FHA is exported by the Sec machinery and transits through the periplasm in an extended conformation. From there it is translocated across the outer membrane by its dedicated transporter FhaC to finally fold into a long β-helix at the cell surface in a progressive manner. In this work, we show that B. pertussis lacking the periplasmic chaperone/protease DegP has a strong growth defect at 37°C, and the integrity of its outer membrane is compromised. While both phenotypes are significantly aggravated by the presence of FHA, the chaperone activity of DegP markedly alleviates the periplasmic stress. In vitro, DegP binds to non-native FHA with high affinity. We propose that DegP chaperones the extended FHA polypeptide in the periplasm and is thus involved in the TPS pathway.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2009.06860.x</identifier><identifier>PMID: 19703106</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Adhesins, Bacterial - metabolism ; Bacteria ; Bacteriology ; Biochemistry ; Biological and medical sciences ; Bordetella ; Bordetella pertussis ; Bordetella pertussis - enzymology ; Bordetella pertussis - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Knockout Techniques ; Genotype & phenotype ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; Microbiology ; Miscellaneous ; Mutation ; Periplasmic Proteins - genetics ; Periplasmic Proteins - metabolism ; Proteases ; Proteins ; Recombinant Proteins - metabolism ; Serine Endopeptidases - genetics ; Serine Endopeptidases - metabolism ; Surface Plasmon Resonance ; Virulence Factors, Bordetella - metabolism</subject><ispartof>Molecular microbiology, 2009-10, Vol.74 (2), p.315-329</ispartof><rights>2009 The Authors. Journal compilation © 2009 Blackwell Publishing Ltd</rights><rights>2009 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Ltd. 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In Gram-negative bacteria, the two-partner secretion (TPS) pathway is dedicated to the secretion of large proteins rich in β-helical structure. The secretion of the filamentous haemagglutinin (FHA), a 230 kDa adhesin of Bordetella pertussis, represents a model TPS system. FHA is exported by the Sec machinery and transits through the periplasm in an extended conformation. From there it is translocated across the outer membrane by its dedicated transporter FhaC to finally fold into a long β-helix at the cell surface in a progressive manner. In this work, we show that B. pertussis lacking the periplasmic chaperone/protease DegP has a strong growth defect at 37°C, and the integrity of its outer membrane is compromised. While both phenotypes are significantly aggravated by the presence of FHA, the chaperone activity of DegP markedly alleviates the periplasmic stress. In vitro, DegP binds to non-native FHA with high affinity. 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Psychology</topic><topic>Gene Knockout Techniques</topic><topic>Genotype & phenotype</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Mutation</topic><topic>Periplasmic Proteins - genetics</topic><topic>Periplasmic Proteins - metabolism</topic><topic>Proteases</topic><topic>Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine Endopeptidases - genetics</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Surface Plasmon Resonance</topic><topic>Virulence Factors, Bordetella - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baud, C</creatorcontrib><creatorcontrib>Hodak, H</creatorcontrib><creatorcontrib>Willery, E</creatorcontrib><creatorcontrib>Drobecq, H</creatorcontrib><creatorcontrib>Locht, C</creatorcontrib><creatorcontrib>Jamin, M</creatorcontrib><creatorcontrib>Jacob-Dubuisson, F</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baud, C</au><au>Hodak, H</au><au>Willery, E</au><au>Drobecq, H</au><au>Locht, C</au><au>Jamin, M</au><au>Jacob-Dubuisson, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of DegP for two-partner secretion in Bordetella</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2009-10</date><risdate>2009</risdate><volume>74</volume><issue>2</issue><spage>315</spage><epage>329</epage><pages>315-329</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Sorting of proteins destined to the surface or the extracellular milieu is mediated by specific machineries, which guide the protein substrates towards the proper route of secretion and determine the compartment in which folding occurs. In Gram-negative bacteria, the two-partner secretion (TPS) pathway is dedicated to the secretion of large proteins rich in β-helical structure. The secretion of the filamentous haemagglutinin (FHA), a 230 kDa adhesin of Bordetella pertussis, represents a model TPS system. FHA is exported by the Sec machinery and transits through the periplasm in an extended conformation. From there it is translocated across the outer membrane by its dedicated transporter FhaC to finally fold into a long β-helix at the cell surface in a progressive manner. In this work, we show that B. pertussis lacking the periplasmic chaperone/protease DegP has a strong growth defect at 37°C, and the integrity of its outer membrane is compromised. While both phenotypes are significantly aggravated by the presence of FHA, the chaperone activity of DegP markedly alleviates the periplasmic stress. In vitro, DegP binds to non-native FHA with high affinity. We propose that DegP chaperones the extended FHA polypeptide in the periplasm and is thus involved in the TPS pathway.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19703106</pmid><doi>10.1111/j.1365-2958.2009.06860.x</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular microbiology, 2009-10, Vol.74 (2), p.315-329 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Adhesins, Bacterial - metabolism Bacteria Bacteriology Biochemistry Biological and medical sciences Bordetella Bordetella pertussis Bordetella pertussis - enzymology Bordetella pertussis - genetics Fundamental and applied biological sciences. Psychology Gene Knockout Techniques Genotype & phenotype Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Microbiology Miscellaneous Mutation Periplasmic Proteins - genetics Periplasmic Proteins - metabolism Proteases Proteins Recombinant Proteins - metabolism Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Surface Plasmon Resonance Virulence Factors, Bordetella - metabolism |
| title | Role of DegP for two-partner secretion in Bordetella |
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