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Article

Defective lipoprotein sorting induces lolA expression through the Rcs stress response phosphorelay system.

Journal of bacteriology - 1 Jul 2012

Tao Kazuyuki, Narita Shin-Ichiro, Tokuda Hajime

Abstract excerpt

The Escherichia coli LolA protein is a lipoprotein-specific chaperone that carries lipoproteins from the inner to the outer membrane. A dominant negative LolA mutant, LolA(I93C/F140C), in which both (93)Ile and (140)Phe are replaced by Cys, binds tightly to the lipoprotein-dedicated ABC transporter LolCDE complex on the inner membrane and therefore inhibits the detachment of outer membrane-specific lipoproteins...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22563052
DOI: 10.1128/JB.00553-12
PMCID: PMC3393486

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Defective lipoprotein sorting induces lolA expression through the Rcs stress response phosphorelay system.PMID 22563052Read ↗

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

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

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

Exploring the relationship between lipoprotein mislocalization and activation of the Rcs signal transduction system in Escherichia coli.Semantic proximity Read ↗

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

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

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

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

<i>Borrelia burgdorferi</i> BB0346 is an Essential, Structurally Variant LolA Homolog that is Primarily Required for Homeostatic Localization of Periplasmic LipoproteinsSemantic proximity Read ↗

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

Structural and functional insights into the Rcs phosphorelaySemantic proximity Read ↗

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