PMID- 22761586
OWN - NLM
STAT- MEDLINE
DCOM- 20120927
LR  - 20211021
IS  - 1553-7404 (Electronic)
IS  - 1553-7390 (Print)
IS  - 1553-7390 (Linking)
VI  - 8
IP  - 6
DP  - 2012 Jun
TI  - Global regulatory functions of the Staphylococcus aureus endoribonuclease III in 
      gene expression.
PG  - e1002782
LID - 10.1371/journal.pgen.1002782 [doi]
LID - e1002782
AB  - RNA turnover plays an important role in both virulence and adaptation to stress 
      in the Gram-positive human pathogen Staphylococcus aureus. However, the molecular 
      players and mechanisms involved in these processes are poorly understood. Here, 
      we explored the functions of S. aureus endoribonuclease III (RNase III), a member 
      of the ubiquitous family of double-strand-specific endoribonucleases. To define 
      genomic transcripts that are bound and processed by RNase III, we performed deep 
      sequencing on cDNA libraries generated from RNAs that were co-immunoprecipitated 
      with wild-type RNase III or two different cleavage-defective mutant variants in 
      vivo. Several newly identified RNase III targets were validated by independent 
      experimental methods. We identified various classes of structured RNAs as RNase 
      III substrates and demonstrated that this enzyme is involved in the maturation of 
      rRNAs and tRNAs, regulates the turnover of mRNAs and non-coding RNAs, and 
      autoregulates its synthesis by cleaving within the coding region of its own mRNA. 
      Moreover, we identified a positive effect of RNase III on protein synthesis based 
      on novel mechanisms. RNase III-mediated cleavage in the 5' untranslated region 
      (5'UTR) enhanced the stability and translation of cspA mRNA, which encodes the 
      major cold-shock protein. Furthermore, RNase III cleaved overlapping 5'UTRs of 
      divergently transcribed genes to generate leaderless mRNAs, which constitutes a 
      novel way to co-regulate neighboring genes. In agreement with recent findings, 
      low abundance antisense RNAs covering 44% of the annotated genes were captured by 
      co-immunoprecipitation with RNase III mutant proteins. Thus, in addition to gene 
      regulation, RNase III is associated with RNA quality control of pervasive 
      transcription. Overall, this study illustrates the complexity of 
      post-transcriptional regulation mediated by RNase III.
FAU - Lioliou, Efthimia
AU  - Lioliou E
AD  - Architecture et Reactivite de l'ARN, Universite de Strasbourg, CNRS, IBMC, 
      Strasbourg, France.
FAU - Sharma, Cynthia M
AU  - Sharma CM
FAU - Caldelari, Isabelle
AU  - Caldelari I
FAU - Helfer, Anne-Catherine
AU  - Helfer AC
FAU - Fechter, Pierre
AU  - Fechter P
FAU - Vandenesch, Francois
AU  - Vandenesch F
FAU - Vogel, Jorg
AU  - Vogel J
FAU - Romby, Pascale
AU  - Romby P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120628
PL  - United States
TA  - PLoS Genet
JT  - PLoS genetics
JID - 101239074
RN  - 0 (5' Untranslated Regions)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Mutant Proteins)
RN  - 0 (RNA, Antisense)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Ribosomal)
RN  - 0 (cold shock protein CS7.4, Bacteria)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 3.1.26.3 (Ribonuclease III)
SB  - IM
MH  - 5' Untranslated Regions
MH  - Bacterial Proteins/genetics/metabolism
MH  - *Gene Expression Regulation, Bacterial
MH  - High-Throughput Nucleotide Sequencing
MH  - Mutant Proteins/genetics/metabolism
MH  - Protein Biosynthesis/genetics
MH  - RNA Processing, Post-Transcriptional/genetics
MH  - RNA Stability/genetics
MH  - RNA, Antisense/genetics/metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA, Ribosomal/genetics
MH  - RNA, Transfer/genetics
MH  - Ribonuclease III/*genetics/*metabolism
MH  - *Staphylococcus aureus/enzymology/genetics
PMC - PMC3386247
COIS- The authors have declared that no competing interests exist.
EDAT- 2012/07/05 06:00
MHDA- 2012/09/28 06:00
PMCR- 2012/06/01
CRDT- 2012/07/05 06:00
PHST- 2011/11/06 00:00 [received]
PHST- 2012/05/09 00:00 [accepted]
PHST- 2012/07/05 06:00 [entrez]
PHST- 2012/07/05 06:00 [pubmed]
PHST- 2012/09/28 06:00 [medline]
PHST- 2012/06/01 00:00 [pmc-release]
AID - PGENETICS-D-11-02374 [pii]
AID - 10.1371/journal.pgen.1002782 [doi]
PST - ppublish
SO  - PLoS Genet. 2012 Jun;8(6):e1002782. doi: 10.1371/journal.pgen.1002782. Epub 2012 
      Jun 28.