NDLI: The proteomic response to mutants of the Escherichia coli RNA degradosome

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Molecular BioSystems Vol - 9 Issue - 3

Molecular BioSystems Vol - 9 Issue - 2

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The proteomic response to mutants of the Escherichia coli RNA degradosome

Content Provider	Royal Society of Chemistry (RSC)
Author	Zhou, Li Wang, Rong Marcotte, Edward M. Vogel, Christine Zhang, Ang B.
Copyright Year	2013
Abstract	The Escherichia coli RNA degradosome recognizes and degrades RNA through the coordination of four main protein components, the endonuclease RNase E, the exonuclease PNPase, the RhlB helicase and the metabolic enzyme enolase. To help our understanding of the functions of the RNA degradosome, we quantified expression changes of >2300 proteins using mass spectrometry based shotgun proteomics in E. coli strains deficient in rhlB, eno, pnp (which displays temperature sensitive growth), or rne(1-602) which encodes a C-terminal truncation mutant of RNase E and is deficient in degradosome assembly. Global protein expression changes are most similar between the pnp and rhlB mutants, confirming the functional relationship between the genes. We observe down-regulation of protein chaperones including GroEL and DnaK (which associate with the degradosome), a decrease in translation related proteins in Δpnp, ΔrhlB and rne(1-602) cells, and a significant increase in the abundance of aminoacyl-tRNA synthetases. Analysis of the observed proteomic changes points to a shared motif, CGCTGG, that may be associated with RNA degradosome targets. Further, our data provide information on the expression modulation of known degradosome-associated proteins, such as DeaD and RNase G, as well as other RNA helicases and RNases – suggesting or confirming functional complementarity in some cases. Taken together, our results emphasize the role of the RNA degradosome in the modulation of the bacterial proteome and provide the first large-scale proteomic description of the response to perturbation of this major pathway of RNA degradation.
Starting Page	750
Ending Page	757
Page Count	8
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	9
Issue Number	4
Journal	Molecular BioSystems
DOI	10.1039/c3mb25513a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Helicase RNA Ribonuclease E Enzyme Escherichia coli Aminoacyl-tRNA Proteome Ribonuclease Shotgun sequencing Protein C-terminus Brian Eno Exonuclease Hsp70 GroEL Proteomics Polynucleotide phosphorylase Mutation Endonuclease Enolase Mass spectrometry
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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A mutation in polynucleotide phosphorylase from Escherichia coli impairing RNA binding and degradosome stability

Phosphorolysis of Aminoacyl-tRNA by Polynucleotide Phosphorylase from Escherichia coli

A mutation in polynucleotide phosphorylase from Escherichia coli impairing RNA binding and degradosome stability

RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex.

Characterization of polynucleotide phosphorylase mutants of Escherichia coli.

RhlB helicase rather than enolase is the β-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)–exoribonucleolytic complex

The Protein Interaction of RNA Helicase B (RhlB) and Polynucleotide Phosphorylase (PNPase) Contributes to the Homeostatic Control of Cysteine in Escherichia coli

Crystal structure of the Escherichia coli RNA degradosome component enolase.

Isolation and Mapping of Polynucleotide Phosphorylase Mutants of Escherichia coli AL !

The proteomic response to mutants of the Escherichia coli RNA degradosome

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