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Article

Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB.

Biochemical and biophysical research communications - 12 Oct 2001

Miyamoto A, Matsuyama Si, Tokuda H

Abstract excerpt

The outer membrane-specific lipoproteins of Escherichia coli are released from the inner membrane as a water-soluble complex with LolA and then transferred to the outer membrane receptor, LolB. LolA thus plays a critical role in the sorting and outer membrane localization of lipoproteins. To dissect the LolA function, the highly conserved residues were subjected to random mutagenesis, followed by selection for a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11587539
DOI: 10.1006/bbrc.2001.5705

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB.PMID 11587539Read ↗

Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli.Semantic proximity Read ↗

Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed {beta}-barrel structures.Semantic proximity Read ↗

Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane.Semantic proximity Read ↗

Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release.Semantic proximity Read ↗

Novel mutations of the LolCDE complex causing outer membrane localization of lipoproteins despite their inner membrane-retention signals.Semantic proximity Read ↗

Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE.Semantic proximity Read ↗

Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA.Semantic proximity Read ↗

Genetic analysis reveals a robust and hierarchical recruitment of the LolA chaperone to the LolCDE lipoprotein transporterSemantic proximity Read ↗

A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals.Semantic proximity Read ↗

Defective lipoprotein sorting induces lolA expression through the Rcs stress response phosphorelay system.Semantic proximity Read ↗

Crystallization and preliminary crystallographic study of the outer-membrane lipoprotein receptor LolB, a member of the lipoprotein localization factors.Semantic proximity Read ↗

Structural investigation of the interaction between LolA and LolB using NMR.Semantic proximity Read ↗

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