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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

Similar Datasets

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

Project description:Effects of rraA overexpression on the global transcript profile of E. coli. This experiment set contains primary data for Figure 5A.

2005-10-13 | E-SMDB-2258 | biostudies-arrayexpress

Effects of rraA deletion on transcription

2005-12-19 | E-GEOD-3869 | biostudies-arrayexpress

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.

2006-03-08 | GSE4383 | GEO

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

2006-03-07 | E-GEOD-4383 | biostudies-arrayexpress

Effects of rraA overexpression on transcription

Project description:Effects of rraA overexpression on the global transcript profile of E. coli. This experiment set contains primary data for Figure 5A, 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 | GSE3870 | GEO

Effects of rraA overexpression on transcription

2005-12-19 | E-GEOD-3870 | biostudies-arrayexpress

Expression of E. coli RNase toxins

Project description:The purpose of this experiment was to identify cleavage sites of E. coli RNase toxins within the E. coli genome.

2020-06-11 | GSE144029 | GEO

RNAseq of E. coli Sakai O157:H7 in the presence of the flexicate compound Λ-5b

Project description:The synthetic flexicate compound Λ-5b shows potent antimicrobial activity against E. coli. In this study we investigated the transcriptomic response of a clinically relevant E. coli, EHEC O157:H7, to a sublethal concentration of the compound.

2019-05-02 | GSE125633 | GEO

Potential regulatory interactions of Escherichia coli RraA protein with DEAD-box helicases.

Project description:Members of the DEAD-box family of RNA helicases contribute to virtually every aspect of RNA metabolism, in organisms from all domains of life. Many of these helicases are constituents of multicomponent assemblies, and their interactions with partner proteins within the complexes underpin their activities and biological function. In Escherichia coli the DEAD-box helicase RhlB is a component of the multienzyme RNA degradosome assembly, and its interaction with the core ribonuclease RNase E boosts the ATP-dependent activity of the helicase. Earlier studies have identified the regulator of ribonuclease activity A (RraA) as a potential interaction partner of both RNase E and RhlB. We present structural and biochemical evidence showing how RraA can bind to, and modulate the activity of RhlB and another E. coli DEAD-box enzyme, SrmB. Crystallographic structures are presented of RraA in complex with a portion of the natively unstructured C-terminal tail of RhlB at 2.8-Å resolution, and in complex with the C-terminal RecA-like domain of SrmB at 2.9 Å. The models suggest two distinct mechanisms by which RraA might modulate the activity of these and potentially other helicases.

| S-EPMC3814787 | biostudies-literature

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