Evidence map›Paper›PMID 31754158›Full record

ArticleScientific reports2019

The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli.

Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  5. 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

12 authors at 3 institutions in 1 country.

Minho LeeDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Minju JooDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Minji SimDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Se-Hoon SimDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Hyun-Lee KimDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Jaejin LeeDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Minkyung RyuDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Ji-Hyun YeomDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Yoonsoo HahnDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea.
Nam-Chul HaDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 08826, Republic of Korea. hanc210@snu.ac.kr.
Jang-Cheon ChoDepartment of Biological Science, Inha University, Incheon, 22212, Republic of Korea. chojc@inha.ac.kr.
Kangseok LeeDepartment of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea. kangseok@cau.ac.kr.
Chung-Ang University · KRInha University · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rapid modulation of RNA function by endoribonucleases during physiological responses to environmental changes is known to be an effective bacterial biochemical adaptation. We report a molecular mechanism underlying the regulation of enolase (eno) expression by two endoribonucleases, RNase G and RNase III, the expression levels of which are modulated by oxygen availability in Escherichia coli. Analyses of transcriptional eno-cat fusion constructs strongly suggested the existence of cis-acting elements in the eno 5' untranslated region that respond to RNase III and RNase G cellular concentrations. Primer extension and S1 nuclease mapping analyses of eno mRNA in vivo identified three eno mRNA transcripts that are generated in a manner dependent on RNase III expression, one of which was found to accumulate in rng-deleted cells. Moreover, our data suggested that RNase III-mediated cleavage of primary eno mRNA transcripts enhanced Eno protein production, a process that involved putative cis-antisense RNA. We found that decreased RNase G protein abundance coincided with enhanced RNase III expression in E. coli grown anaerobically, leading to enhanced eno expression. Thereby, this posttranscriptional up-regulation of eno expression helps E. coli cells adjust their physiological reactions to oxygen-deficient metabolic modes. Our results revealed a molecular network of coordinated endoribonuclease activity that post-transcriptionally modulates the expression of Eno, a key enzyme in glycolysis.

Indexed as

EndoribonucleasesEscherichia coliEscherichia coli ProteinsGene ExpressionGene Expression Regulation, BacterialOxygenPhosphopyruvate HydrataseRibonuclease IIIRNA, BacterialRNA, MessengerRNA Processing, Post-TranscriptionalEndoribonucleasesEscherichia coli ProteinsOxygenPhosphopyruvate HydrataseRibonuclease IIIRNA, BacterialRNA, Messengerrng protein, E coli

Identifiers

PMID31754158
PMCPMC6872547
OpenAlexW2990620192

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.