Evidence map›Paper›PMID 19366704›Full record

ArticleThe Journal of biological chemistry2009

Catalytic properties of RNase BN/RNase Z from Escherichia coli: RNase BN is both an exo- and endoribonuclease.

Tanmay Dutta, Murray P Deutscher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  5. Article
  6. Article
  7. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Messenger RNA degradation in bacterial cells.Annual review of genetics · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Tanmay DuttaDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101, USA.
Murray P Deutscher
University of Miami · US

Funding

RNases and RNA Metabolism in BacteriaR01GM016317 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI DEUTSCHER, MURRAY P · 1985 to 2019
$9.1M
GTP BINDING PROTEIN ACTIVATORF32GM016317 · NIGMS · U.S. NATIONAL INST/CHILD HLTH/HUMAN DEV · PI OOI, CHEAN E · 1993 to 1995
–
NIGMS NIH HHS F32 GM016317NIGMS NIH HHS GM16317NIGMS NIH HHS R01 GM016317
6 · The paper itself

Abstract

Processing of the 3' terminus of tRNA in many organisms is carried out by an endoribonuclease termed RNase Z or 3'-tRNase, which cleaves after the discriminator nucleotide to allow addition of the universal -CCA sequence. In some eubacteria, such as Escherichia coli, the -CCA sequence is encoded in all known tRNA genes. Nevertheless, an RNase Z homologue (RNase BN) is still present, even though its action is not needed for tRNA maturation. To help identify which RNA molecules might be potential substrates for RNase BN, we carried out a detailed examination of its specificity and catalytic potential using a variety of synthetic substrates. We show here that RNase BN is active on both double- and single-stranded RNA but that duplex RNA is preferred. The enzyme displays a profound base specificity, showing no activity on runs of C residues. RNase BN is strongly inhibited by the presence of a 3'-CCA sequence or a 3'-phosphoryl group. Digestion by RNase BN leads to 3-mers as the limit products, but the rate slows on molecules shorter than 10 nucleotides in length. Most interestingly, RNase BN acts as a distributive exoribonuclease on some substrates, releasing mononucleotides and a ladder of digestion products. However, RNase BN also cleaves endonucleolytically, releasing 3' fragments as short as 4 nucleotides. Although the presence of a 3'-phosphoryl group abolishes exoribonuclease action, it has no effect on the endoribonucleolytic cleavages. These data suggest that RNase BN may differ from other members of the RNase Z family, and they provide important information to be considered in identifying a physiological role for this enzyme.

Indexed as

Base SequenceCations, DivalentEndoribonucleasesEscherichia coli ProteinsExoribonucleasesKineticsPhosphoric Diester HydrolasesRecombinant ProteinsRNA, BacterialRNA, TransferSubstrate SpecificityCations, DivalentEndoribonucleasesEscherichia coli ProteinsExoribonucleasesPhosphoric Diester HydrolasesRecombinant Proteinsribonuclease BNRNA, BacterialRNase ZRNA, Transfer

Identifiers

PMID19366704
PMCPMC2708839
OpenAlexW1974232675

What OpenQuestion holds

Textmetadata
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.