Nε-Fatty acylation of Rho GTPases by a MARTX toxin effector
The multifunctional autoprocessing repeats-in-toxin (MARTX) toxins are a family of large toxins that are extensively distributed in bacterial pathogens. MARTX toxins are autocatalytically cleaved to multiple effector domains, which are released into host cells to modulate the host signaling pathways...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2017-10, Vol.358 (6362), p.528-531 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Zhou, Yan Huang, Chunfeng Yin, Li Wan, Muyang Wang, Xiaofei Li, Lin Liu, Yanhua Wang, Zhao Fu, Panhan Zhang, Ni Chen, She Liu, Xiaoyun Shao, Feng Zhu, Yongqun |
| description | The multifunctional autoprocessing repeats-in-toxin (MARTX) toxins are a family of large toxins that are extensively distributed in bacterial pathogens. MARTX toxins are autocatalytically cleaved to multiple effector domains, which are released into host cells to modulate the host signaling pathways. The Rho guanosine triphosphatase (GTPase) inactivation domain (RID), a conserved effector domain of MARTX toxins, is implicated in cell rounding by disrupting the host actin cytoskeleton. We found that the RID is an Nε-fatty acyltransferase that covalently modifies the lysine residues in the C-terminal polybasic region of Rho GTPases. The resulting fatty acylation inhibited Rho GTPases and disrupted Rho GTPase–mediated signaling in the host. Thus, RID can mediate the lysine Nε-fatty acylation of mammalian proteins and represents a family of toxins that harbor N-fatty acyltransferase activities in bacterial pathogens. |
| doi_str_mv | 10.1126/science.aam8659 |
| format | Article |
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MARTX toxins are autocatalytically cleaved to multiple effector domains, which are released into host cells to modulate the host signaling pathways. The Rho guanosine triphosphatase (GTPase) inactivation domain (RID), a conserved effector domain of MARTX toxins, is implicated in cell rounding by disrupting the host actin cytoskeleton. We found that the RID is an Nε-fatty acyltransferase that covalently modifies the lysine residues in the C-terminal polybasic region of Rho GTPases. The resulting fatty acylation inhibited Rho GTPases and disrupted Rho GTPase–mediated signaling in the host. Thus, RID can mediate the lysine Nε-fatty acylation of mammalian proteins and represents a family of toxins that harbor N-fatty acyltransferase activities in bacterial pathogens.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aam8659</identifier><identifier>PMID: 29074776</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Acetyltransferases - chemistry ; Acetyltransferases - metabolism ; Acylation ; Bacterial Toxins - chemistry ; Bacterial Toxins - genetics ; Bacterial Toxins - metabolism ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Protein Domains ; rho GTP-Binding Proteins - metabolism ; Vibrio vulnificus - metabolism</subject><ispartof>Science (American Association for the Advancement of Science), 2017-10, Vol.358 (6362), p.528-531</ispartof><rights>Copyright © 2017 by the American Association for the Advancement of Science</rights><rights>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. 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Thus, RID can mediate the lysine Nε-fatty acylation of mammalian proteins and represents a family of toxins that harbor N-fatty acyltransferase activities in bacterial pathogens.</description><subject>Acetyltransferases - chemistry</subject><subject>Acetyltransferases - metabolism</subject><subject>Acylation</subject><subject>Bacterial Toxins - chemistry</subject><subject>Bacterial Toxins - genetics</subject><subject>Bacterial Toxins - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Protein Domains</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>Vibrio vulnificus - metabolism</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMtKAzEUhoMotlbXrpQs3UybyySZgBsptgr1QqngbshkEpwyM6mTFOyD-Ro-k5GOujoH_u_8cD4AzjEaY0z4xOvKtNqMlWoyzuQBGGIkWSIJoodgiBDlSYYEG4AT79cIxUzSYzAgEolUCD4E149fn8lMhbCDSu9qFSrXQmfh8s3B-epZeeNhETP4cLNcvcLgPqoWGmuNDq47BUdW1d6c9XMEXma3q-ldsnia309vFommHIXE4jLD2upSorIouSgJx0xazEptuM2skjr2GU7iQlJhUkqY4IbRVGtKSUFH4Grfu-nc-9b4kDeV16auVWvc1udYMpFyjCmK6GSP6s553xmbb7qqUd0uxyj_UZb3yvJeWby47Mu3RWPKP_7XUQQu9sDax5__c54ixGlGvwGNQnMM</recordid><startdate>20171027</startdate><enddate>20171027</enddate><creator>Zhou, Yan</creator><creator>Huang, Chunfeng</creator><creator>Yin, Li</creator><creator>Wan, Muyang</creator><creator>Wang, Xiaofei</creator><creator>Li, Lin</creator><creator>Liu, Yanhua</creator><creator>Wang, Zhao</creator><creator>Fu, Panhan</creator><creator>Zhang, Ni</creator><creator>Chen, She</creator><creator>Liu, Xiaoyun</creator><creator>Shao, Feng</creator><creator>Zhu, Yongqun</creator><general>American Association for the Advancement of Science</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>7X8</scope><orcidid>https://orcid.org/0000-0002-4158-5223</orcidid><orcidid>https://orcid.org/0000-0002-3135-6646</orcidid><orcidid>https://orcid.org/0000-0001-5993-9854</orcidid><orcidid>https://orcid.org/0000-0002-0047-7007</orcidid><orcidid>https://orcid.org/0000-0002-4654-1983</orcidid><orcidid>https://orcid.org/0000-0001-7083-5263</orcidid><orcidid>https://orcid.org/0000-0001-9352-7108</orcidid></search><sort><creationdate>20171027</creationdate><title>Nε-Fatty acylation of Rho GTPases by a MARTX toxin effector</title><author>Zhou, Yan ; 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| source | MEDLINE; Science Magazine; Jstor Complete Legacy |
| subjects | Acetyltransferases - chemistry Acetyltransferases - metabolism Acylation Bacterial Toxins - chemistry Bacterial Toxins - genetics Bacterial Toxins - metabolism Crystallography, X-Ray HEK293 Cells Humans Protein Domains rho GTP-Binding Proteins - metabolism Vibrio vulnificus - metabolism |
| title | Nε-Fatty acylation of Rho GTPases by a MARTX toxin effector |
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