Structure and Biological Function of the RNA Pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus

Simon A.J. Messing, Sandra B. Gabelli, Quansheng Liu, Helena Celesnik, Joel G. Belasco, Silvia A. Piñeiro, L. Mario Amzel

Research output: Contribution to journalArticle

Abstract

Until recently, the mechanism of mRNA decay in bacteria was thought to be different from that of eukaryotes. This paradigm changed with the discovery that RppH (ORF176/NudH/YgdP), an Escherichia coli enzyme that belongs to the Nudix superfamily, is an RNA pyrophosphohydrolase that initiates mRNA decay by cleaving pyrophosphate from the 5′-triphosphate. Here we report the 1.9 Å resolution structure of the Nudix hydrolase BdRppH from Bdellovibrio bacteriovorus, a bacterium that feeds on other Gram-negative bacteria. Based on the structure of the enzyme alone and in complex with GTP-Mg2+, we propose a mode of RNA binding similar to that of the nuclear decapping enzyme from Xenopus laevis, X29. In additional experiments, we show that BdRppH can indeed function in vitro and in vivo as an RNA pyrophosphohydrolase. These findings set the basis for the identification of possible decapping enzymes in other bacteria.

Original languageEnglish (US)
Pages (from-to)472-481
Number of pages10
JournalStructure
Volume17
Issue number3
DOIs
StatePublished - Mar 11 2009

    Fingerprint

Keywords

  • RNA
  • SIGNALING

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this