Cyclic di-GMP activation of polynucleotide phosphorylase signal-dependent RNA processing

Jason R. Tuckerman, Gonzalo Gonzalez, Marie Alda Gilles-Gonzalez

Research output: Contribution to journalArticle

90 Scopus citations

Abstract

The second messenger cyclic diguanylic acid (c-di-GMP) is implicated in key lifestyle decisions of bacteria, including biofilm formation and changes in motility and virulence. Some challenges in deciphering the physiological roles of c-di-GMP are the limited knowledge about the cellular targets of c-di-GMP, the signals that control its levels, and the proportion of free cellular c-di-GMP, if any. Here, we identify the target and the regulatory signal for a c-di-GMP-responsive Escherichia coli ribonucleoprotein complex. We show that a direct c-di-GMP target in E. coli is polynucleotide phosphorylase (PNPase), an important enzyme in RNA metabolism that serves as a 3′ polyribonucleotide polymerase or a 3′-to-5′ exoribonuclease. We further show that a complex of polynucleotide phosphorylase with the direct oxygen sensors DosC and DosP can perform oxygen-dependent RNA processing. We conclude that c-di-GMP can mediate signal-dependent RNA processing and that macromolecular complexes can compartmentalize c-di-GMP signaling.

Original languageEnglish (US)
Pages (from-to)633-639
Number of pages7
JournalJournal of Molecular Biology
Volume407
Issue number5
DOIs
StatePublished - Apr 15 2011

Keywords

  • EAL domain
  • GGDEF domain
  • PNPase
  • degradosome
  • oxygen sensor

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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