Evidence map›Paper›PMID 26253740›Full record

ArticleNucleic acids research2015

Linkage of catalysis and 5' end recognition in ribonuclease RNase J.

Xue-Yuan Pei, Patricia Bralley, George H Jones, Ben F Luisi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Frontiers in microbiology · 2023
    Review
  9. Article
  10. Article
  11. Structural and biochemical characteristics of twoThe Journal of biological chemistry · 2020
    Article
  12. Article
  13. Review
  14. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. Regulatory Tools for Controlling Gene Expression in Cyanobacteria.Advances in experimental medicine and biology
    Review
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 2 institutions in 2 countries.

Xue-Yuan PeiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Patricia BralleyDepartment of Biology, Emory University, Atlanta Georgia, USA.
George H JonesDepartment of Biology, Emory University, Atlanta Georgia, USA bfl20@cam.ac.uk.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK bfl20@cam.ac.uk.
Emory University · USUniversity of Cambridge · GB

Funding

Wellcome Trust 076846Wellcome Trust 076846/Z/05/A
6 · The paper itself

Abstract

In diverse bacterial species, the turnover and processing of many RNAs is mediated by the ribonuclease RNase J, a member of the widely occurring metallo-β-lactamase enzyme family. We present crystal structures of Streptomyces coelicolor RNase J with bound RNA in pre- and post-cleavage states, at 2.27 Å and 2.80 Å resolution, respectively. These structures reveal snapshots of the enzyme cleaving substrate directionally and sequentially from the 5' terminus. In the pre-cleavage state, a water molecule is coordinated to a zinc ion pair in the active site but is imperfectly oriented to launch a nucleophilic attack on the phosphate backbone. A conformational switch is envisaged that enables the in-line positioning of the attacking water and may be facilitated by magnesium ions. Adjacent to the scissile bond, four bases are stacked in a tightly sandwiching pocket, and mutagenesis results indicate that this organization helps to drive processive exo-ribonucleolytic cleavage. Like its numerous homologues, S. coelicolor RNase J can also cleave some RNA internally, and the structural data suggest how the preference for exo- versus endo-cleavage mode is linked with recognition of the chemical status of the substrate's 5' end.

Indexed as

Bacterial ProteinsBiocatalysisCatalytic DomainModels, MolecularMutationProtein BindingProtein MultimerizationRibonucleasesRNARNA CleavageStreptomyces coelicolorBacterial ProteinsRibonucleasesRNA

Identifiers

PMID26253740
PMCPMC4652760
OpenAlexW2107295914

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.