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Article

RfaH enhances elongation of Escherichia coli hlyCABD mRNA.

Journal of bacteriology - 1 Apr 1996

Leeds J A, Welch R A

Abstract excerpt

Escherichia coli hlyCABD operons encode the polypeptide component (Hly A) of an extracellular cytolytic toxin, as well as proteins required for its acylation (HlyC) and sec-independent secretion (HlyBD). Previous reports suggested that the E. coli protein RfaH is required for wild-type hemolysin...

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Identifiers

PMID: 8606157
DOI: 10.1128/jb.178.7.1850-1857.1996
PMCID: PMC177878

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-8606157-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

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RfaH enhances elongation of Escherichia coli hlyCABD mRNA.PMID 8606157Read ↗

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Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.Semantic proximity Read ↗

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