Evidence map›Paper›PMID 22893707›Full record

ArticleThe Journal of biological chemistry2012

Exoribonuclease and endoribonuclease activities of RNase BN/RNase Z both function in vivo.

Tanmay Dutta, Arun Malhotra, Murray P Deutscher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  4. Article
  5. Article
  6. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

Tanmay DuttaDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136.
Arun MalhotraDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136.
Murray P DeutscherDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136. Electronic address: mdeutsch@med.miami.edu.
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

Escherichia coli RNase BN, a member of the RNase Z family of endoribonucleases, differs from other family members in that it also can act as an exoribonuclease in vitro. Here, we examine whether this activity of RNase BN also functions in vivo. Comparison of the x-ray structure of RNase BN with that of Bacillus subtilis RNase Z, which lacks exoribonuclease activity, revealed that RNase BN has a narrower and more rigid channel downstream of the catalytic site. We hypothesized that this difference in the putative RNA exit channel might be responsible for the acquisition of exoribonuclease activity by RNase BN. Accordingly, we generated several mutant RNase BN proteins in which residues within a loop in this channel were converted to the corresponding residues present in B. subtilis RNase Z, thus widening the channel and increasing its flexibility. The resulting mutant RNase BN proteins had reduced or were essentially devoid of exoribonuclease activity in vitro. Substitution of one mutant rbn gene (P142G) for wild type rbn in the E. coli chromosome revealed that the exoribonuclease activity of RNase BN is not required for maturation of phage T4 tRNA precursors, a known specific function of this RNase. On the other hand, removal of the exoribonuclease activity of RNase BN in a cell lacking other processing RNases leads to slower growth and affects maturation of multiple tRNA precursors. These findings help explain how RNase BN can act as both an exo- and an endoribonuclease and also demonstrate that its exoribonuclease activity is capable of functioning in vivo, thus widening the potential role of this enzyme in E. coli.

Indexed as

Bacillus subtilisEndoribonucleasesEscherichia coliEscherichia coli ProteinsExoribonucleasesMutationProtein Structure, SecondaryEndoribonucleasesEscherichia coli ProteinsExoribonucleasesribonuclease BNRNase Z

Identifiers

PMID22893707
PMCPMC3471727
OpenAlexW1976377319

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.