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

被引:4
作者
Casinhas, Jorge [1 ]
Matos, Rute G. [1 ]
Haddad, Nabila [2 ]
Arraiano, Cecilia M. [1 ]
机构
[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol Antonio Xavier, Ava Republ, P-2780157 Oeiras, Portugal
[2] Univ Bretagne Loire, SECALIM, INRA, Oniris, F-44307 Nantes, France
关键词
Campylobacter; Ribonucleases; PNPase; RNA metabolism; Foodborne pathogen; COLI POLYNUCLEOTIDE PHOSPHORYLASE; ESCHERICHIA-COLI; RNASE-E; LOW-TEMPERATURE; S1; DOMAIN; CRYSTAL-STRUCTURE; DEGRADATION; EXPRESSION; GROWTH; DEGRADOSOME;
D O I
10.1016/j.biochi.2018.01.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 30 to 50 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. (C) 2018 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
引用
收藏
页码:70 / 79
页数:10
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