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Volume 150, Issue 2

Regulation of RcsA by the ClpYQ (HslUV) protease in Free

Abstract

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 shows that overexpression of ClpQ and ClpY suppresses the mucoid phenotype of a mutant. Since the () gene, involved in capsule synthesis, is activated by RcsA, the reporter construct was used to assay for -galactosidase activity and thus follow RcsA stability. The expression of was increased in double mutants of in combination with or/and mutation(s) compared with the wild-type or single mutants. Overproduction of ClpYQ or ClpQ decreased expression. Additionally, a P– fusion construct showed quantitatively that an inducible RcsA activates expression. The effect of RcsA on expression was shown to be influenced by the ClpYQ activities. Moreover, a translational fusion construct showed higher activity of RcsA–LacZ in a strain than in the wild-type. By contrast, overproduction of cellular ClpYQ resulted in decreased -galactosidase levels of RcsA–LacZ. Taken together, the data indicate that ClpYQ acts as a secondary protease in degrading the Lon substrate RcsA.

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  • Published Online:
Keyword(s): HA, haemagglutinin and MMS, methyl methanesulfonate
SGM
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2004-02-01
2024-04-19
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Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli
Microbiology 150, 437 (2004); https://doi.org/10.1099/mic.0.26446-0
/content/journal/micro/10.1099/mic.0.26446-0
/content/journal/micro/10.1099/mic.0.26446-0
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