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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Transcription profiling of E. coli with rraA deletion, a protein inhibitor of RNase E

ABSTRACT: Effects of rraA deletion on the global transcript profile of E. coli. This experiment set contains primary data for Figure 5B.

ORGANISM(S): Escherichia coli

SUBMITTER: Janos Demeter

PROVIDER: E-SMDB-2257 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli.

Lee Kangseok K Zhan Xiaoming X Gao Junjun J Qiu Ji J Feng Yanan Y Meganathan R R Cohen Stanley N SN Georgiou George G

Cell 20030901 5

Ribonuclease E (RNase E) has a key role in mRNA degradation and the processing of catalytic and structural RNAs in E. coli. We report the discovery of an evolutionarily conserved 17.4 kDa protein, here named RraA (regulator of ribonuclease activity A) that binds to RNase E and inhibits RNase E endonucleolytic cleavages without altering cleavage site specificity or interacting detectably with substrate RNAs. Overexpression of RraA circumvents the effects of an autoregulatory mechanism that normal ...[more]

PMID: 13678585

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Effects of rraA deletion on transcription

Project description:Effects of rraA deletion on the global transcript profile of E. coli. This experiment set contains primary data for Figure 5B, Lee et. al. Cell 2003. An RNA stablity experiment design type examines stability and/or decay of RNA transcripts. Keywords: RNA_stability_design

2005-12-20 | GSE3869 | GEO

Transcription profiling of E. coli overexpressing rraA, a protein inhibitor of RNase E

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RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli

Project description:Abstract: Ribonuclease E (RNase E) has a key role in mRNA degradation and the processing of catalytic and structural RNAs in E. coli. We report the discovery of an evolutionarily conserved 17.4 kDa protein, here named RraA (regulator of ribonuclease activity A) that binds to RNase E and inhibits RNase E endonucleolytic cleavages without altering cleavage site specificity or interacting detectably with substrate RNAs. Overexpression of RraA circumvents the effects of an autoregulatory mechanism that normally maintains the RNase E cellular level within a narrow range, resulting in the genome-wide accumulation of RNase E-targeted transcripts. While not required for RraA action, the C-terminal RNase E region that serves as a scaffold for formation of a multiprotein degradosome complex modulates the inhibition of RNase E catalytic activity by RraA. Our results reveal a possible mechanism for the dynamic regulation of RNA decay and processing by inhibitory RNase binding proteins. This SuperSeries is composed of the SubSeries listed below.

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RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli

Project description:This SuperSeries is composed of the following subset Series: GSE3869: Effects of rraA deletion on transcription GSE3870: Effects of rraA overexpression on transcription Abstract: Ribonuclease E (RNase E) has a key role in mRNA degradation and the processing of catalytic and structural RNAs in E. coli. We report the discovery of an evolutionarily conserved 17.4 kDa protein, here named RraA (regulator of ribonuclease activity A) that binds to RNase E and inhibits RNase E endonucleolytic cleavages without altering cleavage site specificity or interacting detectably with substrate RNAs. Overexpression of RraA circumvents the effects of an autoregulatory mechanism that normally maintains the RNase E cellular level within a narrow range, resulting in the genome-wide accumulation of RNase E-targeted transcripts. While not required for RraA action, the C-terminal RNase E region that serves as a scaffold for formation of a multiprotein degradosome complex modulates the inhibition of RNase E catalytic activity by RraA. Our results reveal a possible mechanism for the dynamic regulation of RNA decay and processing by inhibitory RNase binding proteins. Refer to individual Series

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