PMID- 27821608 OWN - NLM STAT- MEDLINE DCOM- 20170614 LR - 20190329 IS - 1098-5530 (Electronic) IS - 0021-9193 (Print) IS - 0021-9193 (Linking) VI - 199 IP - 2 DP - 2017 Jan 15 TI - Role of RNase Y in Clostridium perfringens mRNA Decay and Processing. LID - 10.1128/JB.00703-16 [doi] LID - e00703-16 AB - RNase Y is a major endoribonuclease that plays a crucial role in mRNA degradation and processing. We study the role of RNase Y in the Gram-positive anaerobic pathogen Clostridium perfringens, which until now has not been well understood. Our study implies an important role for RNase Y-mediated RNA degradation and processing in virulence gene expression and the physiological development of the organism. We began by constructing an RNase Y conditional knockdown strain in order to observe the importance of RNase Y on growth and virulence. Our resulting transcriptome analysis shows that RNase Y affects the expression of many genes, including toxin-producing genes. We provide data to show that RNase Y depletion repressed several toxin genes in C. perfringens and involved the virR-virS two-component system. We also observe evidence that RNase Y is indispensable for processing and stabilizing the transcripts of colA (encoding a major toxin collagenase) and pilA2 (encoding a major pilin component of the type IV pili). Posttranscriptional regulation of colA is known to be mediated by cleavage in the 5' untranslated region (5'UTR), and we observe that RNase Y depletion diminishes colA 5'UTR processing. We show that RNase Y is also involved in the posttranscriptional stabilization of pilA2 mRNA, which is thought to be important for host cell adherence and biofilm formation. IMPORTANCE: RNases have important roles in RNA degradation and turnover in all organisms. C. perfringens is a Gram-positive anaerobic spore-forming bacterial pathogen that produces numerous extracellular enzymes and toxins, and it is linked to digestive disorders and disease. A highly conserved endoribonuclease, RNase Y, affects the expression of hundreds of genes, including toxin genes, and studying these effects is useful for understanding C. perfringens specifically and RNases generally. Moreover, RNase Y is involved in processing specific transcripts, and we observed that this processing in C. perfringens results in the stabilization of mRNAs encoding a toxin and bacterial extracellular apparatus pili. Our study shows that RNase activity is associated with gene expression, helping to determine the growth, proliferation, and virulence of C. perfringens. CI - Copyright (c) 2016 American Society for Microbiology. FAU - Obana, Nozomu AU - Obana N AD - Faculty of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan obana.nozomu.gb@u.tsukuba.ac.jp. FAU - Nakamura, Kouji AU - Nakamura K AD - Faculty of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan. FAU - Nomura, Nobuhiko AU - Nomura N AD - Faculty of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan. LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20161228 PL - United States TA - J Bacteriol JT - Journal of bacteriology JID - 2985120R RN - 0 (Bacterial Proteins) RN - 0 (RNA, Bacterial) RN - 0 (RNA, Messenger) RN - EC 3.1.- (Ribonucleases) RN - EC 3.4.24.3 (Microbial Collagenase) RN - EC 3.4.24.3 (kappa-toxin, Clostridium perfringens) SB - IM MH - Bacterial Proteins/genetics/metabolism MH - Cell Proliferation MH - Clostridium perfringens/*enzymology/genetics/metabolism MH - Gene Expression Regulation, Bacterial/*physiology MH - Microbial Collagenase/genetics/metabolism MH - RNA, Bacterial/genetics/*metabolism MH - RNA, Messenger/genetics/*metabolism MH - Ribonucleases/genetics/*metabolism PMC - PMC5198488 OTO - NOTNLM OT - Clostridium perfringens OT - RNase Y OT - posttranscriptional regulation OT - ribonuclease OT - toxin gene OT - toxin regulation OT - type IV pili EDAT- 2016/11/09 06:00 MHDA- 2017/06/15 06:00 PMCR- 2017/07/15 CRDT- 2016/11/09 06:00 PHST- 2016/09/26 00:00 [received] PHST- 2016/10/27 00:00 [accepted] PHST- 2016/11/09 06:00 [pubmed] PHST- 2017/06/15 06:00 [medline] PHST- 2016/11/09 06:00 [entrez] PHST- 2017/07/15 00:00 [pmc-release] AID - JB.00703-16 [pii] AID - 00703-16 [pii] AID - 10.1128/JB.00703-16 [doi] PST - epublish SO - J Bacteriol. 2016 Dec 28;199(2):e00703-16. doi: 10.1128/JB.00703-16. Print 2017 Jan 15.