Biochemical characterization of Campylobacter jejuni PNPase, an exoribonuclease important for bacterial pathogenicity

Jorge Casinhas, Rute G. Matos, Nabila Haddad, Cecília M. Arraiano

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Bacteria need to promptly respond to environmental changes. Ribonucleases (RNases) are key factors in the adaptation to new environments by enabling a rapid adjustment in RNA levels. The exoribonuclease polynucleotide phosphorylase (PNPase) is essential for low-temperature cell survival, affects the synthesis of proteins involved in virulence and has an important role in swimming, cell adhesion/invasion ability, and chick colonization in C. jejuni. However, the mechanism of action of this ribonuclease is not yet known. In this work we have characterized the biochemical activity of C. jejuni PNPase. Our results demonstrate that Cj-PNP is a processive 3′ to 5′ exoribonuclease that degrades single-stranded RNAs. Its activity is regulated according to the temperature and divalent ions. We have also shown that the KH and S1 domains are important for trimerization, RNA binding, and, consequently, for the activity of Cj-PNP. These findings will be helpful to develop new strategies for fighting against C. jejuni and may be extrapolated to other foodborne pathogens.

Original languageEnglish
Pages (from-to)70-79
Number of pages10
JournalBiochimie
Volume147
DOIs
Publication statusPublished - 1 Apr 2018

Keywords

  • Campylobacter
  • Foodborne pathogen
  • PNPase
  • Ribonucleases
  • RNA metabolism

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