Type III secretion effectors of the IpaH family are E3 ubiquitin ligases
Many bacteria pathogenic for plants or animals, including Shigella spp., which is responsible for shigellosis in humans, use a type III secretion apparatus to inject effector proteins into host cells. Effectors alter cell signaling and host responses induced upon infection; however, their precise bi...
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| Veröffentlicht in: | Cell host & microbe 2007-03, Vol.1 (1), p.77-83 |
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| creator | Rohde, John R Breitkreutz, Ashton Chenal, Alexandre Sansonetti, Philippe J Parsot, Claude |
| description | Many bacteria pathogenic for plants or animals, including Shigella spp., which is responsible for shigellosis in humans, use a type III secretion apparatus to inject effector proteins into host cells. Effectors alter cell signaling and host responses induced upon infection; however, their precise biochemical activities have been elucidated in very few cases. Utilizing Saccharomyces cerevisiae as a surrogate host, we show that the Shigella effector IpaH9.8 interrupts pheromone response signaling by promoting the proteasome-dependent destruction of the MAPKK Ste7. In vitro, IpaH9.8 displayed ubiquitin ligase activity toward ubiquitin and Ste7. Replacement of a Cys residue that is invariant among IpaH homologs of plant and animal pathogens abolished the ubiquitin ligase activity of IpaH9.8. We also present evidence that the IpaH homolog SspH1 from Salmonella enterica can ubiquitinate ubiquitin and PKN1, a previously identified SspH1 interaction partner. This study assigns a function for IpaH family members as E3 ubiquitin ligases. |
| doi_str_mv | 10.1016/j.chom.2007.02.002 |
| format | Article |
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This study assigns a function for IpaH family members as E3 ubiquitin ligases.</description><subject>Animals</subject><subject>Antigens, Bacterial</subject><subject>Antigens, Bacterial - genetics</subject><subject>Antigens, Bacterial - metabolism</subject><subject>Bacterial Proteins</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Transport</subject><subject>Biological Transport - physiology</subject><subject>Genes, Reporter</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mitogen-Activated Protein Kinase Kinases</subject><subject>Mitogen-Activated Protein Kinases</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Pheromones</subject><subject>Pheromones - metabolism</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Protein Kinase C</subject><subject>Protein Kinase C - metabolism</subject><subject>Protein Kinases</subject><subject>Protein Kinases - genetics</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Salmonella enterica</subject><subject>Shigella</subject><subject>Shigella flexneri</subject><subject>Shigella flexneri - genetics</subject><subject>Shigella flexneri - metabolism</subject><subject>Shigella flexneri - pathogenicity</subject><subject>Signal Transduction</subject><subject>Signal Transduction - physiology</subject><subject>Ubiquitin</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>1931-3128</issn><issn>1934-6069</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r4zAUxEXp0n-7X2APi0692X1PsmT5WErbBAK9tGchKdJGwY5dyV7It1-nCe2xpzfwZoaBHyG_EUoElHfb0m36rmQAdQmsBGBn5AobXhUSZHP-obHgyNQluc55CyAE1HhBLlHNWip-RRav-8HT5XJJs3fJj7HfUR-Cd2OfMu0DHTfzezALGkwX2z01ydNHTicb36c4xh1t41-Tff5JfgTTZv_rdG_I29Pj68OiWL08Lx_uV4WrFIyFsRgqG8Sa1xahso1VrhKO2bWwvJbMKCGsdCyglCG4BtZgagENt7XidaX4DSmOvRvT6iHFzqS97k3Ui_uVHkwe_ZQ0oKhA1fIfzv7bo39I_fvk86i7mJ1vW7Pz_ZS1VAJBcvGtERuJjPHDAnY0utTnnHz4nIGgD2D0Vh_A6AMYDUzPYObQn1P7ZDu__oqcSPD_IiWIZQ</recordid><startdate>20070315</startdate><enddate>20070315</enddate><creator>Rohde, John R</creator><creator>Breitkreutz, Ashton</creator><creator>Chenal, Alexandre</creator><creator>Sansonetti, Philippe J</creator><creator>Parsot, Claude</creator><general>Elsevier</general><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>C1K</scope><scope>M7N</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0001-7542-4527</orcidid><orcidid>https://orcid.org/0000-0002-3429-1446</orcidid></search><sort><creationdate>20070315</creationdate><title>Type III secretion effectors of the IpaH family are E3 ubiquitin ligases</title><author>Rohde, John R ; 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Effectors alter cell signaling and host responses induced upon infection; however, their precise biochemical activities have been elucidated in very few cases. Utilizing Saccharomyces cerevisiae as a surrogate host, we show that the Shigella effector IpaH9.8 interrupts pheromone response signaling by promoting the proteasome-dependent destruction of the MAPKK Ste7. In vitro, IpaH9.8 displayed ubiquitin ligase activity toward ubiquitin and Ste7. Replacement of a Cys residue that is invariant among IpaH homologs of plant and animal pathogens abolished the ubiquitin ligase activity of IpaH9.8. We also present evidence that the IpaH homolog SspH1 from Salmonella enterica can ubiquitinate ubiquitin and PKN1, a previously identified SspH1 interaction partner. This study assigns a function for IpaH family members as E3 ubiquitin ligases.</abstract><cop>United States</cop><pub>Elsevier</pub><pmid>18005683</pmid><doi>10.1016/j.chom.2007.02.002</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0001-7542-4527</orcidid><orcidid>https://orcid.org/0000-0002-3429-1446</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell host & microbe, 2007-03, Vol.1 (1), p.77-83 |
| issn | 1931-3128 1934-6069 |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Antigens, Bacterial Antigens, Bacterial - genetics Antigens, Bacterial - metabolism Bacterial Proteins Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry, Molecular Biology Biological Transport Biological Transport - physiology Genes, Reporter Humans Life Sciences Mitogen-Activated Protein Kinase Kinases Mitogen-Activated Protein Kinases Mitogen-Activated Protein Kinases - metabolism Pheromones Pheromones - metabolism Proteasome Endopeptidase Complex Proteasome Endopeptidase Complex - metabolism Protein Kinase C Protein Kinase C - metabolism Protein Kinases Protein Kinases - genetics Protein Kinases - metabolism Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Salmonella enterica Shigella Shigella flexneri Shigella flexneri - genetics Shigella flexneri - metabolism Shigella flexneri - pathogenicity Signal Transduction Signal Transduction - physiology Ubiquitin Ubiquitin - metabolism Ubiquitin-Protein Ligases Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism |
| title | Type III secretion effectors of the IpaH family are E3 ubiquitin ligases |
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