Journal
RNA
Volume 20, Issue 10, Pages 1567-1578Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.043372.113
Keywords
Hfq; Escherichia coli; Clostridium difficile; small noncoding RNAs; gene expression
Categories
Funding
- Centre National de la Recherche Scientifique, University Paris-Diderot [FRE3630]
- Agence Nationale de la Recherche (asSUPYCO) [ANR-12-BSV6-0007-03]
- Initiative d'Excellence program from the French State (Grant DYNAMO) [ANR-11-LABX-0011]
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV6-0007] Funding Source: Agence Nationale de la Recherche (ANR)
Ask authors/readers for more resources
A gene for the Hfq protein is present in the majority of sequenced bacterial genomes. Its characteristic hexameric ring-like core structure is formed by the highly conserved N-terminal regions. In contrast, the C-terminal forms an extension, which varies in length, lacks homology, and is predicted to be unstructured. In Gram-negative bacteria, Hfq facilitates the pairing of sRNAs with their mRNA target and thus affects gene expression, either positively or negatively, and modulates sRNA degradation. In Gram-positive bacteria, its role is still poorly characterized. Numerous sRNAs have been detected in many Gram-positive bacteria, but it is not yet known whether these sRNAs act in association with Hfq. Compared with all other Hfqs, the C. difficile Hfq exhibits an unusual C-terminal sequence with 75% asparagine and glutamine residues, while the N-terminal core part is more conserved. To gain insight into the functionality of the C. difficile Hfq (Cd-Hfq) protein in processes regulated by sRNAs, we have tested the ability of Cd-Hfq to fulfill the functions of the E. coli Hfq (Ec-Hfq) by examining various functions associated with Hfq in both positive and negative controls of gene expression. We found that Cd-Hfq substitutes for most but not all of the tested functions of the Ec-Hfq protein. We also investigated the role of the C-terminal part of the Hfq proteins. We found that the C-terminal part of both Ec-Hfq and Cd-Hfq is not essential but contributes to some functions of both the E. con and C. difficile chaperons.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available