Evidence map›Paper›PMID 34788459›Full record

ArticleNucleic acids research2022

RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids.

Hyunjee Lee, HyeokJin Cho, Jooyoung Kim, Sua Lee, Jungmin Yoo, Daeho Park, Gwangrog Lee

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Functional Insight into hTRIR.Current molecular medicine · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 1 institution in 1 country.

Hyunjee LeeSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
HyeokJin ChoSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Jooyoung KimSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Sua LeeSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Jungmin YooSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Daeho ParkSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Gwangrog LeeSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.ORCID 0000-0002-1720-8524
Gwangju Institute of Science and Technology · KR

Funding

Environmental Health Perspectives, NIEHS27302C0031 · NIEHS · 2008 to 2008
$1.2M
2016 SETAC Asia/Pacific ConferenceR13ES027302 · NIEHS · SOCIETY/ENVIRONMENTAL TOXICOLOGY/CHEM · PI MENZIE, CHARLES · 2016 to 2016
$6k
NIEHS NIH HHS 27302C0031
6 · The paper itself

Abstract

RNase H is involved in fundamental cellular processes and is responsible for removing the short stretch of RNA from Okazaki fragments and the long stretch of RNA from R-loops. Defects in RNase H lead to embryo lethality in mice and Aicardi-Goutieres syndrome in humans, suggesting the importance of RNase H. To date, RNase H is known to be a non-sequence-specific endonuclease, but it is not known whether it performs other functions on the structural variants of RNA:DNA hybrids. Here, we used Escherichia coli RNase H as a model, and examined its catalytic mechanism and its substrate recognition modes, using single-molecule FRET. We discovered that RNase H acts as a processive exoribonuclease on the 3' DNA overhang side but as a distributive non-sequence-specific endonuclease on the 5' DNA overhang side of RNA:DNA hybrids or on blunt-ended hybrids. The high affinity of previously unidentified double-stranded (ds) and single-stranded (ss) DNA junctions flanking RNA:DNA hybrids may help RNase H find the hybrid substrates in long genomic DNA. Our study provides new insights into the multifunctionality of RNase H, elucidating unprecedented roles of junctions and ssDNA overhang on RNA:DNA hybrids.

Indexed as

Ribonuclease HRNAAnimalsDNAEndonucleasesEndoribonucleasesEscherichia coliMiceDNAEndonucleasesEndoribonucleasesRibonuclease HRNA

Identifiers

PMID34788459
PMCPMC8886854
OpenAlexW3213735419

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.