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Article

Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli.

Microbiology (Reading, England) - 1 Feb 2004

Kuo Mei-Shiue, Chen Kuei-Peng, Wu Whi Fin

Abstract excerpt

Escherichia coli ClpYQ protease and Lon protease possess a redundant function for degradation of SulA, a cell division inhibitor. An experimental cue implied that the capsule synthesis activator RcsA, a known substrate of Lon, is probably a specific substrate for the ClpYQ protease. This paper sh...

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Identifiers

PMID: 14766922
DOI: 10.1099/mic.0.26446-0

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BAD

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14766922-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli.PMID 14766922Read ↗

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