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Outer Membrane Protein Insertion by the β-barrel Assembly Machine.

Author(s): Ricci, Dante P; Silhavy, Thomas J

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dc.contributor.authorRicci, Dante P-
dc.contributor.authorSilhavy, Thomas J-
dc.date.accessioned2023-12-12T15:36:47Z-
dc.date.available2023-12-12T15:36:47Z-
dc.date.issued2019-03en_US
dc.identifier.citationRicci, Dante P, Silhavy, Thomas J. (2019). Outer Membrane Protein Insertion by the β-barrel Assembly Machine. EcoSal Plus, 8 (2), 10.1128/ecosalplus.esp-0035-2018en_US
dc.identifier.issn2324-6200-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1zs2kc9h-
dc.description.abstractLike all outer membrane (OM) constituents, integral OM β-barrel proteins in Gram-negative bacteria are synthesized in the cytoplasm and trafficked to the OM, where they are locally assembled into the growing OM by the ubiquitous β-barrel assembly machine (Bam). While the identities and structures of all essential and accessory Bam components have been determined, the basic mechanism of Bam-assisted OM protein integration remains elusive. Here we review mechanistic analyses of OM β-barrel protein folding and Bam dynamics and summarize recent insights that inform a general model for OM protein recognition and assembly by the Bam complex.en_US
dc.languageengen_US
dc.language.isoen_USen_US
dc.relation.ispartofEcoSal Plusen_US
dc.rightsAuthor's manuscripten_US
dc.titleOuter Membrane Protein Insertion by the β-barrel Assembly Machine.en_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1128/ecosalplus.esp-0035-2018-
dc.identifier.eissn2324-6200-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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