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3‧ Exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli

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TLDR
A model is proposed that identifies a structural feature present in all the small, stable RNAs of E. coli, and describes how this structure together with the RNases influences the common mechanism for 3' maturation.
Abstract
In addition to tRNA and 5S RNA, Escherichia coli contains several other small, stable RNA species; these are M1, 10Sa, 6S, and 4.5S RNA. Although these RNAs are initially synthesized as precursor molecules, relatively little is known about their maturation. The data presented here show that 3′ exoribonucleolytic trimming is required for the final maturation of each of these molecules. As found previously with tRNA, but not 5S RNA, any one of a number of exoribonucleases can carry out the trimming reaction in vivo, although RNases T and PH are most effective. In their absence, large amounts of immature molecules accumulate for most of the RNAs, and these can be converted to the mature forms in vitro by the purified RNases. A model is proposed that identifies a structural feature present in all the small, stable RNAs of E. coli, and describes how this structure together with the RNases influences the common mechanism for 3′ maturation.

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A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans

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Functions of the exosome in rRNA, snoRNA and snRNA synthesis.

TL;DR: It is concluded that the exosome is involved in the processing of many RNA substrates and that different components can have distinct functions.
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Exoribonuclease superfamilies: structural analysis and phylogenetic distribution

TL;DR: This analysis analyzes the structure and phylogenetic distribution of the known exoribonucleases and identifies common motifs that can be used to characterize newly-discovered exorIBonucle enzymes, and correct some previously misassigned proteins.
References
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Journal ArticleDOI

Catalytic activity of an RNA molecule prepared by transcription in vitro

TL;DR: The RNA moiety M1RNA of ribonuclease P from Escherichia coli and the unprocessed transcript prepared in vitro of the gene for M1 RNA can both perform the cleavage reactions of the canonical enzyme in the absence of the protein moiety.
Journal ArticleDOI

C-terminal Extension of Truncated Recombinant Proteins in Escherichia coli with a 10Sa RNA Decapeptide

TL;DR: Peptide mapping, electrospray ionization-mass spectrometry, and automated N- and C-terminal sequencing identified a peptide (“tag” peptide), encoded by a small metabolically stable RNA of E. coli attached to truncated C termini of the recombinant protein.
Journal ArticleDOI

Maturation Pathways for E. coli tRNA Precursors: A Random Multienzyme Process In Vivo

Zhongwei Li, +1 more
- 09 Aug 1996 - 
TL;DR: The surprising conclusion from this work is that tRNA maturation is a stochastic process that lacks a defined order and that can proceed with a variety of alternative 3' processing nucleases.
Journal ArticleDOI

Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli.

TL;DR: The reaction catalyzing by the holoenzyme with p4.5S as substrate has a much lower Km value than that catalyzed by M1 RNA with the same substrate, indicating that the protein subunit plays a crucial role in the recognition of p4 .5S.
Journal ArticleDOI

Nucleotide sequence of the gene encoding the RNA subunit (M1 RNA) of ribonuclease P from Escherichia coli

TL;DR: The gene encoding the RNA subunit (M1 RNA) of RNAase P (EC 3.26.5) from Escherichia coli has been isolated, and its complete nucleotide sequence, including flanking regions, has been determined.
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