{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["110(10)"],"submitter":["Pavlova O"],"funding":["Intramural NIH HHS"],"pubmed_abstract":["Autotransporters are bacterial virulence factors that contain an N-terminal extracellular (\"passenger\") domain and a C-terminal β barrel (\"β\") domain that anchors the protein to the outer membrane. The β domain is required for passenger domain secretion, but its exact role in autotransporter biogenesis is unclear. Here we describe insights into the function of the β domain that emerged from an analysis of mutations in the Escherichia coli O157:H7 autotransporter EspP. We found that the G1066A and G1081D mutations slightly distort the structure of the β domain and delay the initiation of passenger domain translocation. Site-specific photocrosslinking experiments revealed that the mutations slow the insertion of the β domain into the outer membrane, but do not delay the binding of the β domain to the factor that mediates the insertion reaction (the Bam complex). Our results demonstrate that the β domain does not simply target the passenger domain to the outer membrane, but promotes translocation when it reaches a specific stage of assembly. Furthermore, our results provide evidence that the Bam complex catalyzes the membrane integration of β barrel proteins in a multistep process that can be perturbed by minor structural defects in client proteins."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["E938-47"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3593871"],"repository":["biostudies-literature"],"pubmed_title":["Mechanistic link between β barrel assembly and the initiation of autotransporter secretion."],"pmcid":["PMC3593871"],"pubmed_authors":["Pavlova O","Ieva R","Bernstein HD","Peterson JH"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.","description":"Autotransporters are bacterial virulence factors that contain an N-terminal extracellular (\"passenger\") domain and a C-terminal β barrel (\"β\") domain that anchors the protein to the outer membrane. The β domain is required for passenger domain secretion, but its exact role in autotransporter biogenesis is unclear. Here we describe insights into the function of the β domain that emerged from an analysis of mutations in the Escherichia coli O157:H7 autotransporter EspP. We found that the G1066A and G1081D mutations slightly distort the structure of the β domain and delay the initiation of passenger domain translocation. Site-specific photocrosslinking experiments revealed that the mutations slow the insertion of the β domain into the outer membrane, but do not delay the binding of the β domain to the factor that mediates the insertion reaction (the Bam complex). Our results demonstrate that the β domain does not simply target the passenger domain to the outer membrane, but promotes translocation when it reaches a specific stage of assembly. Furthermore, our results provide evidence that the Bam complex catalyzes the membrane integration of β barrel proteins in a multistep process that can be perturbed by minor structural defects in client proteins.","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Mar","modification":"2025-04-19T09:05:59.44Z","creation":"2019-03-27T01:05:52Z"},"accession":"S-EPMC3593871","cross_references":{"pubmed":["23431155"],"doi":["10.1073/pnas.1219076110"]}}