Evidence map›Paper›PMID 19627501›Full record

ArticleMolecular microbiology2009

RNase II is important for A-site mRNA cleavage during ribosome pausing.

Fernando Garza-Sánchez, Shinichiro Shoji, Kurt Fredrick, Christopher S Hayes

Abstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  3. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  4. Article
  5. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  6. Ribosome-based quality control of mRNA and nascent peptides.Wiley interdisciplinary reviews. RNA · 2017
    Review
  7. Article
  8. Article
  9. Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 3 countries.

Fernando Garza-SánchezDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9610, USA.
Shinichiro Shoji
Kurt Fredrick
Christopher S Hayes
Czech Academy of Sciences, Institute of Microbiology · CZInstitut thématique Génétique, génomique et bioinformatique · FRUniversity of California, Santa Barbara · US

Funding

Molecular analysis of accurate ribosomal translocationR01GM072528 · NIGMS · OHIO STATE UNIVERSITY · PI Kurt L Fredrick · 2005 to 2026
$5.8M
Molecular determinants of A-site mRNA cleavage ribosomeR01GM078634 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI HAYES, CHRISTOPHER S. · 2006 to 2014
$2.5M
NIGMS NIH HHS GM072528NIGMS NIH HHS GM078634NIGMS NIH HHS R01 GM072528NIGMS NIH HHS R01 GM078634
6 · The paper itself

Abstract

In Escherichia coli, translational arrest can elicit cleavage of codons within the ribosomal A site. This A-site mRNA cleavage is independent of RelE, and has been proposed to be an endonucleolytic activity of the ribosome. Here, we show that the 3'-->5' exonuclease RNase II plays an important role in RelE-independent A-site cleavage. Instead of A-site cleavage, translational pausing in DeltaRNase II cells produces transcripts that are truncated +12 and +28 nucleotides downstream of the A-site codon. Deletions of the genes encoding polynucleotide phosphorylase (PNPase) and RNase R had little effect on A-site cleavage. However, PNPase overexpression restored A-site cleavage activity to DeltaRNase II cells. Purified RNase II and PNPase were both unable to directly catalyse A-site cleavage in vitro. Instead, these exonucleases degraded ribosome-bound mRNA to positions +18 and +24 nucleotides downstream of the ribosomal A site respectively. Finally, a stable structural barrier to exoribonuclease activity inhibited A-site cleavage when introduced immediately downstream of paused ribosomes. These results demonstrate that 3'-->5' exonuclease activity is an important prerequisite for efficient A-site cleavage. We propose that RNase II degrades mRNA to the downstream border of paused ribosomes, facilitating cleavage of the A-site codon by an unknown RNase.

Indexed as

Protein BiosynthesisBase SequenceEscherichia coliEscherichia coli ProteinsExoribonucleasesGene DeletionMolecular Sequence DataPolyribonucleotide NucleotidyltransferaseRibosomesRNA, MessengerEscherichia coli Proteinsexoribonuclease IIExoribonucleasesPolyribonucleotide NucleotidyltransferaseRNA, Messenger

Identifiers

PMID19627501
PMCPMC2753246
OpenAlexW1996104434

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.