Evidence map›Paper›PMID 27875308›Full record

ArticleThe Journal of biological chemistry2016

Growth Phase-dependent Variation of RNase BN/Z Affects Small RNAs: REGULATION OF 6S RNA.

Hua Chen, Tanmay Dutta, Murray P Deutscher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Probing the conformational changes ofFrontiers in molecular biosciences · 2023
    Article
  4. RNA (New York, N.Y.) · 2022
    Article
  5. Article
  6. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  11. Review
  12. Genes Contributing toFrontiers in cellular and infection microbiology · 2017
    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.

Hua ChenFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101.
Tanmay DuttaFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101.
Murray P DeutscherFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101 m.deutscher@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 R01 GM016317
6 · The paper itself

Abstract

RNase BN, the RNase Z family member in E. coli, can participate in the processing of tRNA precursors. However, this function only becomes apparent when other processing enzymes are absent, raising the question of its primary physiological role. Here, we show that RNase BN itself is subject to growth phase-dependent regulation, because both rbn mRNA and RNase BN protein are at their highest levels in early exponential phase, but then decrease dramatically and are essentially absent in stationary phase. As a consequence of this variation, certain small RNAs, such as 6S RNA, remain low in exponential phase cells, and increase greatly in stationary phase. RNase BN affects 6S RNA abundance by decreasing its stability in exponential phase. RNase BN levels increase rapidly as cells exit stationary phase and are primarily responsible for the decrease in 6S RNA that accompanies this process. Purified RNase BN directly cleaves 6S RNA as shown by in vitro assays, and the 6S RNA:pRNA duplex is an even more favorable substrate of RNase BN. The exoribonuclease activity of RNase BN is unnecessary because all its action on 6S RNA is due to endonucleolytic cleavages. These data indicate that RNase BN plays an important role in determining levels of the global transcription regulator, 6S RNA, throughout the growth cycle.

Indexed as

EndoribonucleasesEscherichia coli K12Escherichia coli ProteinsExoribonucleasesRNA, BacterialRNA, MessengerRNA StabilityRNA, Untranslated6S RNAEndoribonucleasesEscherichia coli ProteinsExoribonucleasesribonuclease BNRNA, BacterialRNA, MessengerRNase ZRNA, UntranslatedbacteriaEscherichia coli (E. coli)ribonucleaseRNA metabolismRNA turnoversmall RNA

Identifiers

PMID27875308
PMCPMC5159504
OpenAlexW2550463279

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.