A novel mechanism for ribonuclease regulation: Transfer-messenger RNA (tmRNA) and its associated protein SmpB regulate the stability of RNase R

Wenxing Liang, Murray P Deutscher

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The amount of RNase R, an important degradative exoribonuclease, increases 3-10-fold under a variety of stress conditions. This elevation is due to posttranslational regulation in which the highly unstable RNase R protein becomes stabilized during stress. Here we identify two components of the trans-translation machinery, transfer-messenger RNA (tmRNA) and SmpB, that are responsible for the short half-life of RNase R in exponential phase cells. The absence of either lengthens the half-life of RNaseR in vivo >6-fold. SmpB directly interacts with RNase R in vitro and is stimulated by tmRNA. The C-terminal region of RNase R, encompassing its basic region and adjacent S1 domain are required for the interaction; their removal eliminates binding and stabilizes RNase R in vivo. However, the binding of SmpB and tmRNA does not alter RNase R activity. These data define a previously unknown regulatory process in which the stability of an RNase is determined by its interaction with an RNA and an RNA-associated protein.

Original languageEnglish
Pages (from-to)29054-29058
Number of pages5
JournalJournal of Biological Chemistry
Volume285
Issue number38
DOIs
StatePublished - Sep 17 2010

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Ribonucleases
Transfer RNA
Messenger RNA
Half-Life
Exoribonucleases
RNA
small protein B
ribonuclease R
Machinery
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

A novel mechanism for ribonuclease regulation : Transfer-messenger RNA (tmRNA) and its associated protein SmpB regulate the stability of RNase R. / Liang, Wenxing; Deutscher, Murray P.

In: Journal of Biological Chemistry, Vol. 285, No. 38, 17.09.2010, p. 29054-29058.

Research output: Contribution to journalArticle

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