Staphylococcus aureus RNAIII binds to two distant regions of coa mRNA to arrest translation and promote mRNA degradation.

Bibliographic Details
Title: Staphylococcus aureus RNAIII binds to two distant regions of coa mRNA to arrest translation and promote mRNA degradation.
Authors: Clément Chevalier, Sandrine Boisset, Cédric Romilly, Benoit Masquida, Pierre Fechter, Thomas Geissmann, François Vandenesch, Pascale Romby
Source: PLoS Pathogens, Vol 6, Iss 3, p e1000809 (2010)
Publisher Information: Public Library of Science (PLoS), 2010.
Publication Year: 2010
Collection: LCC:Immunologic diseases. Allergy
LCC:Biology (General)
Subject Terms: Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
More Details: Staphylococcus aureus RNAIII is the intracellular effector of the quorum sensing system that temporally controls a large number of virulence factors including exoproteins and cell-wall-associated proteins. Staphylocoagulase is one major virulence factor, which promotes clotting of human plasma. Like the major cell surface protein A, the expression of staphylocoagulase is strongly repressed by the quorum sensing system at the post-exponential growth phase. Here we used a combination of approaches in vivo and in vitro to analyze the mechanism used by RNAIII to regulate the expression of staphylocoagulase. Our data show that RNAIII represses the synthesis of the protein through a direct binding with the mRNA. Structure mapping shows that two distant regions of RNAIII interact with coa mRNA and that the mRNA harbors a conserved signature as found in other RNAIII-target mRNAs. The resulting complex is composed of an imperfect duplex masking the Shine-Dalgarno sequence of coa mRNA and of a loop-loop interaction occurring downstream in the coding region. The imperfect duplex is sufficient to prevent the formation of the ribosomal initiation complex and to repress the expression of a reporter gene in vivo. In addition, the double-strand-specific endoribonuclease III cleaves the two regions of the mRNA bound to RNAIII that may contribute to the degradation of the repressed mRNA. This study validates another direct target of RNAIII that plays a role in virulence. It also illustrates the diversity of RNAIII-mRNA topologies and how these multiple RNAIII-mRNA interactions would mediate virulence regulation.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1553-7366
1553-7374
Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20300607/pdf/?tool=EBI; https://doaj.org/toc/1553-7366; https://doaj.org/toc/1553-7374
DOI: 10.1371/journal.ppat.1000809
Access URL: https://doaj.org/article/991d745a3ba84f7eb3eccac0f951b25f
Accession Number: edsdoj.991d745a3ba84f7eb3eccac0f951b25f
Database: Directory of Open Access Journals
More Details
ISSN:15537366
15537374
DOI:10.1371/journal.ppat.1000809
Published in:PLoS Pathogens
Language:English