scholarly journals Ribonuclease E: Chopping Knife and Sculpting Tool

2017 ◽  
Vol 65 (1) ◽  
pp. 3-4 ◽  
Author(s):  
Joel G. Belasco
Keyword(s):  
Ribonuclease E

scholarly journals Maturation of UTR-Derived sRNAs Is Modulated during Adaptation to Different Growth Conditions

2021 ◽  
Vol 22 (22) ◽  
pp. 12260
Author(s):  
Daniel-Timon Spanka ◽  
Gabriele Klug
Keyword(s):  
Growth Conditions ◽  
Global Scale ◽  
Rnase E ◽  
Bacterial Gene ◽  
Ribonuclease E ◽  
Mrna Targets ◽  
Small Regulatory Rnas ◽  
The Stability ◽  
Ngs Data

Small regulatory RNAs play a major role in bacterial gene regulation by binding their target mRNAs, which mostly influences the stability or translation of the target. Expression levels of sRNAs are often regulated by their own promoters, but recent reports have highlighted the presence and importance of sRNAs that are derived from mRNA 3′ untranslated regions (UTRs). In this study, we investigated the maturation of 5′ and 3′ UTR-derived sRNAs on a global scale in the facultative phototrophic alphaproteobacterium Rhodobacter sphaeroides. Including some already known UTR-derived sRNAs like UpsM or CcsR1-4, 14 sRNAs are predicted to be located in 5′ UTRs and 16 in 3′ UTRs. The involvement of different ribonucleases during maturation was predicted by a differential RNA 5′/3′ end analysis based on RNA next generation sequencing (NGS) data from the respective deletion strains. The results were validated in vivo and underline the importance of polynucleotide phosphorylase (PNPase) and ribonuclease E (RNase E) during processing and maturation. The abundances of some UTR-derived sRNAs changed when cultures were exposed to external stress conditions, such as oxidative stress and also during different growth phases. Promoter fusions revealed that this effect cannot be solely attributed to an altered transcription rate. Moreover, the RNase E dependent cleavage of several UTR-derived sRNAs varied significantly during the early stationary phase and under iron depletion conditions. We conclude that an alteration of ribonucleolytic processing influences the levels of UTR-derived sRNAs, and may thus indirectly affect their mRNA targets.

scholarly journals Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome

1998 ◽  
Vol 12 (17) ◽  
pp. 2770-2781 ◽  
Author(s):  
N. F. Vanzo ◽  
Y. S. Li ◽  
B. Py ◽  
E. Blum ◽  
C. F. Higgins ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Interactions ◽  
Ribonuclease E ◽  
Rna Degradosome

ribonuclease E 3.1.26.12

2013 ◽  
pp. 559-593
Author(s):  
Dietmar Schomburg ◽  
Ida Schomburg
Keyword(s):  
Ribonuclease E

scholarly journals Ribonuclease E provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA.

1994 ◽  
Vol 8 (24) ◽  
pp. 3021-3031 ◽  
Author(s):  
P Alifano ◽  
F Rivellini ◽  
C Piscitelli ◽  
C M Arraiano ◽  
C B Bruni ◽  
...  
Keyword(s):  
Ribonuclease P ◽  
Ribonuclease E ◽  
Polycistronic Mrna

scholarly journals Regulation of ribonuclease E activity by the L4 ribosomal protein ofEscherichia coli

2009 ◽  
Vol 106 (3) ◽  
pp. 864-869 ◽  
Author(s):  
Dharam Singh ◽  
Ssu-Jean Chang ◽  
Pei-Hsun Lin ◽  
Olga V. Averina ◽  
Vladimir R. Kaberdin ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Ofescherichia Coli ◽  
Ribonuclease E

scholarly journals The First Small-Molecule Inhibitors of Members of the Ribonuclease E Family

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Louise Kime ◽  
Helen A. Vincent ◽  
Deena M. A. Gendoo ◽  
Stefanie S. Jourdan ◽  
Colin W. G. Fishwick ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Small Molecules ◽  
Small Molecule ◽  
High Throughput Screening ◽  
Small Molecule Inhibitors ◽  
Rnase E ◽  
Ribonuclease E ◽  
New Antibiotics ◽  
Drug Leads ◽  
Number Of Bacteria

Abstract The Escherichia coli endoribonuclease RNase E is central to the processing and degradation of all types of RNA and as such is a pleotropic regulator of gene expression. It is essential for growth and was one of the first examples of an endonuclease that can recognise the 5′-monophosphorylated ends of RNA thereby increasing the efficiency of many cleavages. Homologues of RNase E can be found in many bacterial families including important pathogens, but no homologues have been identified in humans or animals. RNase E represents a potential target for the development of new antibiotics to combat the growing number of bacteria that are resistant to antibiotics in use currently. Potent small molecule inhibitors that bind the active site of essential enzymes are proving to be a source of potential drug leads and tools to dissect function through chemical genetics. Here we report the use of virtual high-throughput screening to obtain small molecules predicted to bind at sites in the N-terminal catalytic half of RNase E. We show that these compounds are able to bind with specificity and inhibit catalysis of Escherichia coli and Mycobacterium tuberculosis RNase E and also inhibit the activity of RNase G, a paralogue of RNase E.

Ribonuclease E is a 5′-end-dependent endonuclease

Nature ◽  
10.1038/27246 ◽  
1998 ◽  
Vol 395 (6703) ◽  
pp. 720-724 ◽  
Author(s):  
George A. Mackie
Keyword(s):  
Ribonuclease E ◽  
Dependent Endonuclease
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