Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function

被引:20
作者
Caillet, Joel [1 ,2 ]
Gracia, Celine [1 ,2 ]
Fontaine, Fanette [1 ,2 ]
Hajnsdorf, Eliane [1 ,2 ]
机构
[1] Univ Paris Diderot, Sorbonne Paris Cite, Inst Biol Physicochim, CNRS FRE3630, F-75005 Paris, France
[2] Univ Paris Diderot, Sorbonne Paris Cite, Inst Biol Physicochim, UPR9073, F-75005 Paris, France
关键词
Hfq; Escherichia coli; Clostridium difficile; small noncoding RNAs; gene expression; MESSENGER-RNA TARGETS; SMALL NONCODING RNAS; BINDING-PROTEIN HFQ; BACTERIAL SMALL RNA; C-TERMINAL DOMAIN; LISTERIA-MONOCYTOGENES; STAPHYLOCOCCUS-AUREUS; POSTTRANSCRIPTIONAL REGULATION; TRANSLATIONAL REPRESSION; INTERACTION SURFACES;
D O I
10.1261/rna.043372.113
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
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.
引用
收藏
页码:1567 / 1578
页数:12
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