Regulation of the small regulatory RNA MicA by ribonuclease III: a target-dependent pathway

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Abstract

MicA is a trans-encoded small non-coding RNA, which downregulates porin-expression in stationary-phase. In this work, we focus on the role of endoribonucleases III and E on Salmonella typhimurium sRNA MicA regulation. RNase III is shown to regulate MicA in a target-coupled way, while RNase E is responsible for the control of free MicA levels in the cell. We purified both Salmonella enzymes and demonstrated that in vitro RNase III is only active over MicA when in complex with its targets (whether ompA or lamB mRNAs). In vivo, MicA is demonstrated to be cleaved by RNase III in a coupled way with ompA mRNA. On the other hand, RNase E is able to cleave unpaired MicA and does not show a marked dependence on its 5' phosphorylation state. The main conclusion of this work is the existence of two independent pathways for MicA turnover. Each pathway involves a distinct endoribonuclease, having a different role in the context of the fine-tuned regulation of porin levels. Cleavage of MicA by RNase III in a target-dependent fashion, with the concomitant decay of the mRNA target, strongly resembles the eukaryotic RNAi system, where RNase III-like enzymes play a pivotal role.
Original languageUnknown
Pages (from-to)2918-2930
JournalNucleic Acids Research
Volume39
Issue numberNA
DOIs
Publication statusPublished - 1 Jan 2011

Cite this

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title = "Regulation of the small regulatory RNA MicA by ribonuclease III: a target-dependent pathway",
abstract = "MicA is a trans-encoded small non-coding RNA, which downregulates porin-expression in stationary-phase. In this work, we focus on the role of endoribonucleases III and E on Salmonella typhimurium sRNA MicA regulation. RNase III is shown to regulate MicA in a target-coupled way, while RNase E is responsible for the control of free MicA levels in the cell. We purified both Salmonella enzymes and demonstrated that in vitro RNase III is only active over MicA when in complex with its targets (whether ompA or lamB mRNAs). In vivo, MicA is demonstrated to be cleaved by RNase III in a coupled way with ompA mRNA. On the other hand, RNase E is able to cleave unpaired MicA and does not show a marked dependence on its 5' phosphorylation state. The main conclusion of this work is the existence of two independent pathways for MicA turnover. Each pathway involves a distinct endoribonuclease, having a different role in the context of the fine-tuned regulation of porin levels. Cleavage of MicA by RNase III in a target-dependent fashion, with the concomitant decay of the mRNA target, strongly resembles the eukaryotic RNAi system, where RNase III-like enzymes play a pivotal role.",
keywords = "OUTER-MEMBRANE PROTEINS, GENE-EXPRESSION, OMPA MESSENGER-RNA, ESCHERICHIA-COLI K-12, TRANSLATIONAL INHIBITION, ENVELOPE STRESS-RESPONSE, SALMONELLA-TYPHIMURIUM, SMALL NONCODING RNAS, STAPHYLOCOCCUS-AUREUS RNAIII, ANTISENSE RNA",
author = "Domingues, {Susana Margarida} and Arraiano, {Cecilia Maria} and Viegas, {Sandra Cristina}",
year = "2011",
month = "1",
day = "1",
doi = "10.1093/nar/gkq1239",
language = "Unknown",
volume = "39",
pages = "2918--2930",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
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TY - JOUR

T1 - Regulation of the small regulatory RNA MicA by ribonuclease III: a target-dependent pathway

AU - Domingues, Susana Margarida

AU - Arraiano, Cecilia Maria

AU - Viegas, Sandra Cristina

PY - 2011/1/1

Y1 - 2011/1/1

N2 - MicA is a trans-encoded small non-coding RNA, which downregulates porin-expression in stationary-phase. In this work, we focus on the role of endoribonucleases III and E on Salmonella typhimurium sRNA MicA regulation. RNase III is shown to regulate MicA in a target-coupled way, while RNase E is responsible for the control of free MicA levels in the cell. We purified both Salmonella enzymes and demonstrated that in vitro RNase III is only active over MicA when in complex with its targets (whether ompA or lamB mRNAs). In vivo, MicA is demonstrated to be cleaved by RNase III in a coupled way with ompA mRNA. On the other hand, RNase E is able to cleave unpaired MicA and does not show a marked dependence on its 5' phosphorylation state. The main conclusion of this work is the existence of two independent pathways for MicA turnover. Each pathway involves a distinct endoribonuclease, having a different role in the context of the fine-tuned regulation of porin levels. Cleavage of MicA by RNase III in a target-dependent fashion, with the concomitant decay of the mRNA target, strongly resembles the eukaryotic RNAi system, where RNase III-like enzymes play a pivotal role.

AB - MicA is a trans-encoded small non-coding RNA, which downregulates porin-expression in stationary-phase. In this work, we focus on the role of endoribonucleases III and E on Salmonella typhimurium sRNA MicA regulation. RNase III is shown to regulate MicA in a target-coupled way, while RNase E is responsible for the control of free MicA levels in the cell. We purified both Salmonella enzymes and demonstrated that in vitro RNase III is only active over MicA when in complex with its targets (whether ompA or lamB mRNAs). In vivo, MicA is demonstrated to be cleaved by RNase III in a coupled way with ompA mRNA. On the other hand, RNase E is able to cleave unpaired MicA and does not show a marked dependence on its 5' phosphorylation state. The main conclusion of this work is the existence of two independent pathways for MicA turnover. Each pathway involves a distinct endoribonuclease, having a different role in the context of the fine-tuned regulation of porin levels. Cleavage of MicA by RNase III in a target-dependent fashion, with the concomitant decay of the mRNA target, strongly resembles the eukaryotic RNAi system, where RNase III-like enzymes play a pivotal role.

KW - OUTER-MEMBRANE PROTEINS

KW - GENE-EXPRESSION

KW - OMPA MESSENGER-RNA

KW - ESCHERICHIA-COLI K-12

KW - TRANSLATIONAL INHIBITION

KW - ENVELOPE STRESS-RESPONSE

KW - SALMONELLA-TYPHIMURIUM

KW - SMALL NONCODING RNAS

KW - STAPHYLOCOCCUS-AUREUS RNAIII

KW - ANTISENSE RNA

U2 - 10.1093/nar/gkq1239

DO - 10.1093/nar/gkq1239

M3 - Article

VL - 39

SP - 2918

EP - 2930

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - NA

ER -