Evidence map›Paper›PMID 20023028›Full record

ArticleJournal of bacteriology2010

Escherichia coli RNase R has dual activities, helicase and RNase.

Naoki Awano, Vaishnavi Rajagopal, Mark Arbing, Smita Patel, John Hunt, Masayori Inouye, Sangita Phadtare

Abstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

45 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. HELZ2 RegulatesCirculation · 2026
    Article
  3. RNA exoribonucleases in E. coli.Archives of microbiology · 2026
    Review
  4. Genome-wide Screening of the Escherichia coli Keio Knockout Collection Identifies Genetic Determinants of Epetraborole Hypersusceptibility.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Article
  5. Article
  6. Article
  7. Exoribonuclease RNase R protects AntarcticApplied and environmental microbiology · 2023
    Article
  8. Article
  9. A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Biosensor-Assisted Adaptive Laboratory Evolution for Violacein Production.International journal of molecular sciences · 2021
    Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 3 institutions in 1 country.

Naoki AwanoDepartment of Biochemistry, Robert Wood Johnson Medical School, UMDNJ, CABM, 679 Hoes Lane, Piscataway, New Jersey 08854, USA.
Vaishnavi Rajagopal
Mark Arbing
Smita Patel
John Hunt
Masayori Inouye
Sangita Phadtare
Johnson University · USColumbia University · USJohns Hopkins University · US

Funding

MECHANISTIC STUDIES OF HEXAMERIC HELICASESR01GM055310 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PATEL, SMITA S · 1997 to 2015
$4.6M
NIGMS NIH HHS R01 GM055310
6 · The paper itself

Abstract

In Escherichia coli, the cold shock response occurs when there is a temperature downshift from 37 degrees C to 15 degrees C, and this response is characterized by induction of several cold shock proteins, including the DEAD-box helicase CsdA, during the acclimation phase. CsdA is involved in a variety of cellular processes. Our previous studies showed that the helicase activity of CsdA is critical for its function in cold shock acclimation of cells and that the only proteins that were able to complement its function were another helicase, RhlE, an RNA chaperone, CspA, and a cold-inducible exoribonuclease, RNase R. Interestingly, other major 3'-to-5' processing exoribonucleases of E. coli, such as polynucleotide phosphorylase and RNase II, cannot complement the cold shock function of CsdA. Here we carried out a domain analysis of RNase R and showed that this protein has two distinct activities, RNase and helicase, which are independent of each other and are due to different domains. Mutant RNase R proteins that lack the RNase activity but exhibit the helicase activity were able to complement the cold shock function of CsdA, suggesting that only the helicase activity of RNase R is essential for complementation of the cold shock function of CsdA. We also observed that in vivo deletion of the two cold shock domains resulted in a loss of the ability of RNase R to complement the cold shock function of CsdA. We further demonstrated that RNase R exhibits helicase activity in vitro independent of its RNase activity. Our results shed light on the unique properties of RNase R and how it is distinct from other exoribonucleases in E. coli.

Indexed as

Escherichia coliEscherichia coli ProteinsExoribonucleasesGenetic Complementation TestMutant ProteinsMutationProtein Structure, TertiaryRNA HelicasesEscherichia coli ProteinsExoribonucleasesMutant ProteinsRNA Helicasesrnr protein, E coli

Identifiers

PMID20023028
PMCPMC2820863
OpenAlexW2137353773

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.