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Article

Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery.

Molecular microbiology - 1 Nov 2000

Bost S, Silva F, Rudaz C, Belin D

Abstract excerpt

A chimeric protein containing the uncleaved signal sequence of plasminogen activators inhibitor-2 (PAI2) fused to alkaline phosphatase (AP) interferes with Escherichia coli protein export and arrests growth. Suppressors of this toxicity include secG mutations that define the Thr-41-Leu-42-Phe-43 (TLF) domain of SecG. These mutations slow down the export of PAI2-AP. Another construct encoding a truncated PAI2...

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Identifiers

PMID: 11069681
DOI: 10.1046/j.1365-2958.2000.02153.x

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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.

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