Reversible acetylation on Lys501 regulates the activity of RNase II

Limin Song, Guangyuan Wang, Arun Malhotra, Murray P Deutscher, Wenxing Liang

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

RNase II, a 3′ to 5′ processive exoribonuclease, is the major hydrolytic enzyme in Escherichia coli accounting for ∼90% of the total activity. Despite its importance, little is actually known about regulation of this enzyme. We show here that one residue, Lys501, is acetylated in RNase II. This modification, reversibly controlled by the acetyltransferase Pka, and the deacetylase CobB, affects binding of the substrate and thus decreases the catalytic activity of RNase II. As a consequence, the steady-state level of target RNAs of RNase II may be altered in the cells. We also find that under conditions of slowed growth, the acetylation level of RNase II is elevated and the activity of RNase II decreases, emphasizing the importance of this regulatory process. These findings indicate that acetylation can regulate the activity of a bacterial ribonuclease.

Original languageEnglish (US)
Pages (from-to)1979-1988
Number of pages10
JournalNucleic Acids Research
Volume44
Issue number5
DOIs
StatePublished - Feb 4 2016

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Acetylation
Acetyltransferases
Enzymes
Ribonucleases
exoribonuclease II
Escherichia coli
Growth

ASJC Scopus subject areas

  • Genetics

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Reversible acetylation on Lys501 regulates the activity of RNase II. / Song, Limin; Wang, Guangyuan; Malhotra, Arun; Deutscher, Murray P; Liang, Wenxing.

In: Nucleic Acids Research, Vol. 44, No. 5, 04.02.2016, p. 1979-1988.

Research output: Contribution to journalArticle

Song, Limin ; Wang, Guangyuan ; Malhotra, Arun ; Deutscher, Murray P ; Liang, Wenxing. / Reversible acetylation on Lys501 regulates the activity of RNase II. In: Nucleic Acids Research. 2016 ; Vol. 44, No. 5. pp. 1979-1988.
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