Ribonuclease E is a bacterial ribonuclease that participates in the processing of ribosomal RNA (9S to 5S rRNA) and the chemical degradation of bulk cellular RNA. RNase E was suggested to be a part of the cell membrane protein complex, as …

2012年12月14日 · RNase E is a central player in both stable-RNA processing and mRNA decay. It initiates the processing of about two-thirds of all pre-tRNAs and the decay of most mRNAs. It also...

The activity of RNase E can be directed and modulated by signals provided through regulatory RNAs that guide the enzyme to specific transcripts that are to be silenced. Early in its evolutionary history, RNase E acquired a natively unfolded appendage …

2025年1月13日 · RNase E is a pivotal enzyme in bacterial RNA metabolism, playing a key role in the processing and degradation of RNA. Its function is essential for maintaining cellular homeostasis by regulating RNA levels and ensuring proper gene expression.

RNase E, the main component of RNA degradosome in Escherichia coli, plays an important role in mRNA degradation and RNA transcript processing (4, 5). It recognizes and cuts single-stranded RNA with numerous AU bases, thereby cleaving mRNA …

As noted above, RNase E serves many important functions in E. coli cells, acting to process or degrade essentially every type of RNA molecule. RNase E also is an essential enzyme, indicating that no other RNase is able to take over at least one of its many functions in its absence.

1998年10月15日 · Ribonuclease (RNase) E (ref. 1), a single-strand-specific endonuclease 2, 3, 4 that is found in a multi-enzyme complex known as the ‘degradosome’ 5, 6, 7, initiates the degradation of many mRNAs...

The essential endoribonuclease of E. coli is named RNase E. RNase E-related enzymes are present in many bacterial species and are thought to be the primary decay-initiating enzyme in these organisms. RNase E is a 5′-end-dependent endonuclease, that is, it binds to the 5′ end of an mRNA and then locates a target site at which it cleaves ...

Here we show using RNA-seq analyses of ribonuclease-deficient strains in vivo and a 5′-sensor mutant of RNase E in vitro that, contrary to current models, 5′-monophosphate-independent, ‘direct entry’ cleavage is a major pathway for degrading and processing RNA.

2019年11月1日 · Here, using recombinantly expressed and purified proteins, site-directed mutagenesis, and RNA cleavage and protein cross-linking assays, we investigated Hfq-independent RNA decay by RNase E. Exploring its RNA substrate preferences in the absence of Hfq, we observed that RNase E preferentially cleaves AU-rich sites of single-stranded regions …

4 天之前 · Purified RNase E 1-529-Flag, RNase E 1-588-Flag, RNase E 572-1057-Flag, RNase E 572-1057_NDPRmut - Flag, or RNase E 572-1057_AR1mut - Flag fusion proteins (20-25 µg each) were diluted in buffer H to a final volume of 100 µL and incubated with the magnetic beads for 1 hour at 4 °C on a rotating device. After the incubation, the beads were ...

2021年3月31日 · RNase Y and RNase E are disparate endoribonucleases that govern global mRNA turnover/processing in the two evolutionary distant bacteria Bacillus subtilis and Escherichia coli, respectively. The two enzymes share a similar in vitro cleavage specificity and subcellular localization.

In this Review, I summarize the major roles of RNase E in RNA processing and decay and discuss the various mechanisms that regulate its activity. I also propose a new model to rationalize the mechanism of RNase E action in the context of its localization in the bacterial cell.

RNase E enzyme from E. coli cells, and herein describe the isolation and some characterization of this enzyme and the reactions which lead from 9 S to p5.

RNase-E-Dependent sRNA Biogenesis and Maturation in Bacteria. We identify RNase E as a key factor both for the biogenesis of many 3′ UTR-derived sRNAs and for the maturation of active sRNAs from their non-coding precursors. This establishes RNase E cleavage as a second major pathway for the biogenesis of Hfq-dependent sRNAs (Figure 7A). As ...

5 天之前 · f A549 cells were treated with RNase R (3 U of RNase R/μg RNA for 10 min), and qPCR was performed to measure the expression levels of circPLCE1 and PLCE1 mRNAs. ... e After circPLCE1 silencing/overexpression in A549 cells, ATG12, P62 and LC3B protein expression levels were detected via WB analysis.

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RNase E is an essential endoribonuclease involved in RNA processing and mRNA degradation. The N-terminal half of the protein encompasses the catalytic domain; the C-terminal half is the scaffold for the assembly of the multienzyme RNA degradosome.

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