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April 23, 2003Nucleic Acids ResearchOpen Access

RNA structure-dependent uncoupling of substrate recognition and cleavage by Escherichia coli ribonuclease III

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Population

In vitro model using Escherichia coli ribonuclease III and RNA derived from T7 phage R1.1 RNase III substrate

Comparison

R1.1[CL3B] RNA vs R1.1 RNA (wild-type substrate)

Design

Preclinical

Authors

ICIrina Calin‐JagemanDominican University

Discussion

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Overview

Uncoupling of RNase III binding and cleavage by RNA motifs; leaves open in vivo roles and applications in bacterial RNA engineering.

Structured PICO

P
Population
In vitro model using Escherichia coli ribonuclease III and RNA derived from T7 phage R1.1 RNase III substrate
I
Intervention
R1.1[CL3B] RNA (mutated RNA with a bulge-helix-bulge motif)
C
Comparator
R1.1 RNA (wild-type substrate)
O
Outcome
Cleavage resistance and binding affinitysurrogate

The study provides direct evidence that E. coli RNase III can bind RNA without cleaving it, mediated by specific RNA structural motifs.

Cite This Study

Irina Calin‐Jageman (2003) studied this question.

synapsesocial.com/papers/6a70b85dfebe604dd7097c87https://doi.org/10.1093/nar/gkg329
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1A conserved double-stranded RNA-binding domain.1992 · 544 citations
  2. 2Mutational analysis of a ribonuclease III processing signal1993 · 50 citations
  3. 3Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects1993 · 69 citations
  4. 4Comparative sequence analysis of ribonucleases HII, III, II PH and D1997 · 184 citations