Evidence map›Paper›PMID 26847092›Full record

ArticleNucleic acids research2016

Reversible acetylation on Lys501 regulates the activity of RNase II.

Limin Song, Guangyuan Wang, Arun Malhotra, Murray P Deutscher, Wenxing Liang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 83 citations in OpenAlex.

  1. RNA exoribonucleases in E. coli.Archives of microbiology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  9. Review
  10. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    Review
  20. 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

5 authors at 2 institutions in 2 countries.

Limin SongThe Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
Guangyuan WangShandong Province Key Laboratory of Applied Mycology, College of Life Sciences, Qingdao Agricultural University, Qingdao 266109, China.
Arun MalhotraDepartment of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33101, USA.
Murray P DeutscherDepartment of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33101, USA.
Wenxing LiangThe Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China wliang1@qau.edu.cn.
Qingdao Agricultural University · CNUniversity 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
NIGMS NIH HHS GM16317NIGMS NIH HHS R01 GM016317
6 · The paper itself

Abstract

RNase II, a 3' to 5' processive exoribonuclease, is the major hydrolytic enzyme in Escherichia coli accounting for ∼90% of the total activity. Despite its importance, little is actually known about regulation of this enzyme. We show here that one residue, Lys501, is acetylated in RNase II. This modification, reversibly controlled by the acetyltransferase Pka, and the deacetylase CobB, affects binding of the substrate and thus decreases the catalytic activity of RNase II. As a consequence, the steady-state level of target RNAs of RNase II may be altered in the cells. We also find that under conditions of slowed growth, the acetylation level of RNase II is elevated and the activity of RNase II decreases, emphasizing the importance of this regulatory process. These findings indicate that acetylation can regulate the activity of a bacterial ribonuclease.

Indexed as

Gene Expression Regulation, BacterialProtein Processing, Post-TranslationalAcetylationAcetyltransferasesCatalytic DomainEscherichia coliEscherichia coli ProteinsExoribonucleasesLysineProtein BindingRNA, BacterialSirtuinsAcetyltransferasescobB protein, E ColiEscherichia coli Proteinsexoribonuclease IIExoribonucleasesLysineRNA, BacterialSirtuins

Identifiers

PMID26847092
PMCPMC4797298
OpenAlexW2271589648

What OpenQuestion holds

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LicenceCC BY-NC
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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.