Outer membrane protein insertion by the β-barrel assembly machine

Dante P. Ricci, Thomas J. Silhavy

Research output: Chapter in Book/Report/Conference proceedingChapter


The presence in Gram-negative bacteria of an extracytoplasmic outer membrane (OM), which is distinct from the inner membrane (IM) both in constitution and in function, presents a complex topological problem, as all proteinaceous and lipidic OM components are synthesized cytoplasmically (1). In order to reach their destination in the growing OM, these components must translocate across the IM and traverse the aqueous, crowded periplasmic space. This problem is solved through a series of semi-independent and highly conserved transport pathways that coordinate the efficient delivery and integration of all OM constituents.

Original languageEnglish (US)
Title of host publicationProtein Secretion in Bacteria
Number of pages11
ISBN (Electronic)9781683670445
ISBN (Print)9781683670278
StatePublished - Jan 1 2019

All Science Journal Classification (ASJC) codes

  • General Immunology and Microbiology


  • BamA assisted β-barrel folding
  • Catalytic mechanism
  • Outer membrane constituents
  • Outer membrane protein insertion
  • Periplasmic chaperone
  • β-barrel assembly machine
  • β-strand exchange model


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