Outer membrane protein insertion by the β-barrel assembly machine

Dante P. Ricci; Thomas J. Silhavy

doi:10.1128/9781683670285.ch8

Outer membrane protein insertion by the β-barrel assembly machine

Dante P. Ricci, Thomas J. Silhavy

Molecular Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

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 language	English (US)
Title of host publication	Protein Secretion in Bacteria
Publisher	wiley
Pages	91-101
Number of pages	11
ISBN (Electronic)	9781683670445
ISBN (Print)	9781683670278
DOIs	https://doi.org/10.1128/9781683670285.ch8
State	Published - Jan 1 2019

All Science Journal Classification (ASJC) codes

General Immunology and Microbiology

Keywords

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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10.1128/9781683670285.ch8

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abstract = "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.",

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AU - Silhavy, Thomas J.

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N2 - 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.

AB - 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.

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KW - β-barrel assembly machine

KW - β-strand exchange model

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BT - Protein Secretion in Bacteria

PB - wiley

ER -

Outer membrane protein insertion by the β-barrel assembly machine

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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