Molecular recognition between<i>Escherichia coli</i>enolase and ribonuclease E

Nurmohamed, Salima; McKay, Adam R.; Robinson, Carol V.; Luisi, Ben F.

doi:10.1107/s0907444910030015

Cited by 21 publications

(27 citation statements)

References 22 publications

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“…The scaffold domain binds to the RhlB helicase, the phosphorolytic exoribonuclease polynucleotide phosphorylase, and enolase. The RNase E microdomain resides within the scaffolding section and consists of a ϳ28 amino acid conserved region that binds to a dimeric interface between two enolase proteins to promote the decay of specific mRNAs in E. coli (30,31,34,35). Given the large size of IntS1, it may simultaneously interact with multiple other members of the integrator complex in an analogous way to the scaffolding domain of RNase E. Our data support a model where binding of IntS12 to IntS1 alters IntS1 confirmation, allowing further interaction(s) with other proteins and activation of the complex.…”

Section: Discussionmentioning

confidence: 99%

Functional Analysis of the Integrator Subunit 12 Identifies a Microdomain That Mediates Activation of the Drosophila Integrator Complex

Chen

Waltenspiel

Warren

et al. 2013

Journal of Biological Chemistry

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Background: Small nuclear RNA (snRNA) 3Ј end processing is carried out by the poorly understood integrator complex. Results: An essential microdomain within IntS12 binds IntS1 and is required for integrator complex activity. Conclusion: A small binding interface between the largest and smallest integrator subunits is critical for snRNA processing. Significance: These data uncover the unexpected findings that the IntS12 PHD finger is nearly dispensable for snRNA processing, whereas a microdomain is required.

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Section: Discussionmentioning

confidence: 99%

Functional Analysis of the Integrator Subunit 12 Identifies a Microdomain That Mediates Activation of the Drosophila Integrator Complex

Chen

Waltenspiel

Warren

et al. 2013

Journal of Biological Chemistry

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“…In the thermophilic bacterium Carboxydothermus ferrireducens, an NADPH-dependent oxidoreductase has been found to reduce Fe(III), Cr(VI), AQDS, and quinines (Onyenwoke et al, 2009). Enolase is responsible for the reversible catalysis of 2-phospho-D-glycerate (2PGA) and phosphoenolpyruvate (PEP) in glycolysis and gluconeogenesis (Nurmohamed et al, 2010). The enzyme is highly conserved in archaea, bacteria, and eukaryotes with similar catalytic properties (Nurmohamed et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Induction of Cr(VI) reduction activity in an Anoxybacillus strain under heat stress: a biochemical and proteomic study

Paul

Jain

Mitra

et al. 2012

FEMS Microbiol Lett

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A bacterial strain, designated as TSB‐6, was isolated from the sediments of a Tantloi (India) hot spring at 65 °C. The strain showed 98% 16S rRNA gene sequence similarity with Anoxybacillus kualawohkensis strain KW12 and was found to grow optimally at 37 °C. However, growing cells, cell suspensions, and cell‐free extracts from 65 °C cultures showed higher Cr(VI) reduction activities when assayed at either 37 or 65 °C than those obtained from 37 °C cultures. On fractionation of extracts from cells grown at 65 °C, the chromate reductase activity assayed at 65 °C was found mostly in the soluble fraction. When log‐phase cells growing at 37 °C were shifted to 65 °C, the stressed cells produced larger quantities of reactive oxygen species. Consequently, growth of the cells was retarded, but specific Cr(VI) reduction activity increased. 2D gel electrophoresis followed by MALDI‐TOF MS/MS identified the proteins whose expression level changed as a result of heat stress. The upregulated set included proteins involved in cellular metabolism of sugar, nucleotide, amino acids, lipids and vitamins, oxidoreductase activity, and protein folding. The downregulated proteins are also involved in cellular metabolism, DNA binding, and environmental signal processing.

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“…Since enolase is essential under anaerobic conditions, we wondered whether enolase bound to RNase E/degradosomes plays a role in anaerobically induced cell filamentation. We generated another strain (Rned823-850) in which the chromosome region encoding amino acid residues 823-850 of RNase E [constituting the RNase E microdomain for enolase recognition (15)] was deleted. The Rned823-850 strain could host PNPase and RhlB helicase, but not enolase, in degradosomes under both aerobic and anaerobic growth conditions (Fig.…”

Section: Resultsmentioning

confidence: 99%

Escherichia coliresponds to environmental changes using enolasic degradosomes and stabilized DicF sRNA to alter cellular morphology

Murashko

Lin‐Chao

2017

Proc. Natl. Acad. Sci. U.S.A.

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Escherichia coli RNase E is an essential enzyme that forms multicomponent ribonucleolytic complexes known as "RNA degradosomes." These complexes consist of four major components: RNase E, PNPase, RhlB RNA helicase, and enolase. However, the role of enolase in the RNase E/degradosome is not understood. Here, we report that presence of enolase in the RNase E/degradosome under anaerobic conditions regulates cell morphology, resulting in E. coli MG1655 cell filamentation. Under anaerobic conditions, enolase bound to the RNase E/degradosome stabilizes the small RNA (sRNA) DicF, i.e., the inhibitor of the cell division gene ftsZ, through chaperon protein Hfq-dependent regulation. RNase E/enolase distribution changes from membraneassociated patterns under aerobic to diffuse patterns under anaerobic conditions. When the enolase-RNase E/degradosome interaction is disrupted, the anaerobically induced characteristics disappear. We provide a mechanism by which E. coli uses enolase-bound degradosomes to switch from rod-shaped to filamentous form in response to anaerobiosis by regulating RNase E subcellular distribution, RNase E enzymatic activity, and the stability of the sRNA DicF required for the filamentous transition. In contrast to E. coli nonpathogenic strains, pathogenic E. coli strains predominantly have multiple copies of sRNA DicF in their genomes, with cell filamentation previously being linked to bacterial pathogenesis. Our data suggest a mechanism for bacterial cell filamentation during infection under anaerobic conditions. RNase E | RNA decay | protein subcellular distribution | anaerobic conditions | cell shape P osttranscriptional regulation of RNAs is an important molecular mechanism for controlling gene expression, requiring various ribonucleases (RNases), including RNase E, which is an essential single-stranded endo-RNase involved in RNA processing and decay (1). RNase E has N-terminal catalytic and C-terminal scaffolding domains (2), with the latter responsible for assembling multicomponent ribonucleolytic complexes termed "RNA degradosomes." Degradosomes consist of RNase E, PNPase 3′→5′ exoribonuclease, RhlB RNA helicase, and the glycolytic enzyme enolase (3, 4). Therefore, they can act on RNA internally (by RNase E) and/or externally (by PNPase) to catalyze the degradation of RNA into short fragments. Immunogold electron microscopy has shown that degradosomes exist in vivo and are tethered to the cytoplasmic membrane through the N-terminal region of RNase E (5). Binding of the N-terminal catalytic domain (amino acids 1-499) to the membrane stabilizes protein structure and increases both RNA cleavage activity and substrate affinity (6). Global analyses of aerobic Escherichia coli RNA degradosome functioning using DNA microarrays showed that decay of some mRNAs in vivo depends on the action of assembled degradosomes, whereas other mRNAs are impacted by degradosome proteins functioning independently of the complex (7-9). Some minor components of the degradosome, such as the inhibitors of RNase E, RraA and ...

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Molecular recognition betweenEscherichia colienolase and ribonuclease E

Abstract: The glycolytic enzyme enolase associates with the endoribonuclease RNase E in Escherichia coli and many other bacterial species. The crystal structure of the complex reveals the basis for the molecular recognition and provides clues as to the possible function of the interaction.

Cited by 21 publications

References 22 publications

Functional Analysis of the Integrator Subunit 12 Identifies a Microdomain That Mediates Activation of the Drosophila Integrator Complex

Functional Analysis of the Integrator Subunit 12 Identifies a Microdomain That Mediates Activation of the Drosophila Integrator Complex

Induction of Cr(VI) reduction activity in an Anoxybacillus strain under heat stress: a biochemical and proteomic study

Escherichia coliresponds to environmental changes using enolasic degradosomes and stabilized DicF sRNA to alter cellular morphology

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