Journal
FEMS MICROBIOLOGY LETTERS
Volume 336, Issue 2, Pages 139-147Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.12000.x
Keywords
bacterial stress response; RNase E; cold shock
Categories
Funding
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1020739] Funding Source: National Science Foundation
- NIGMS NIH HHS [R01 GM099790] Funding Source: Medline
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Yersinia polynucleotide phosphorylase (PNPase), a 3'5' exoribonuclease, has been shown to affect growth during several stress responses. In Escherichia coli, PNPase is one of the subunits of a multiprotein complex known as the degradosome, but also has degradosome-independent functions. The carboxy-terminus of E. coli ribonuclease E (RNase E) serves as the scaffold upon which PNPase, enolase (a glycolytic enzyme), and RhlB helicase all have been shown to bind. In the yersiniae, only PNPase has thus far been shown to physically interact with RNase E. We show by bacterial two-hybrid and co-immunoprecipitation assays that RhlB and enolase also interact with RNase E. Interestingly, although PNPase is required for normal growth at cold temperatures, assembly of the yersiniae degradosome was not required. However, degradosome assembly was required for growth in the presence of reactive oxygen species. These data suggest that while the Yersinia pseudotuberculosis PNPase plays a role in the oxidative stress response through a degradosome-dependent mechanism, PNPase's role during cold stress is degradosome-independent.
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