Evidence map›Paper›PMID 18337749›Full record

ArticleThe EMBO journal2008

Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.

Marcin Nowotny, Susana M Cerritelli, Rodolfo Ghirlando, Sergei A Gaidamakov, Robert J Crouch, Wei Yang

Abstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
–field-weighted citation impact
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

75 citing papers in PubMed.

  1. Article
  2. Article
  3. Sequence and structural alignments reveal insights into ANKLE2 evolution and function.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. RNA-DNA hybrid binding domain broadens the editing window of base editors.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. AFM Imaging Reveals MicroRNA-132 to be a Positive Regulator of Synaptic Functions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  18. Article
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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

6 authors.

Marcin NowotnyLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Susana M Cerritelli
Rodolfo Ghirlando
Sergei A Gaidamakov
Robert J Crouch
Wei Yang

Funding

Factors Influencing Genetic Transcription Initiation And TerminationZIAHD000068 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI CROUCH, ROBERT J · 2009 to 2025
$22.0M
Structural and mechanistic studies of RNase H and HIV reverse transcriptaseZIADK036144 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2009 to 2021
$4.2M
FACTORS INFLUENCING GENETIC TRANSCRIPTION-INITIATION AND TERMINATIONZ01HD000068 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI CROUCH, ROBERT J · 1985 to 2008
$2.2M
Structural and mechanistic studies of RNase H and HIV reverse transcriptaseZ01DK036144 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2007 to 2008
$601k
Intramural NIH HHS
6 · The paper itself

Abstract

Human RNase H1 contains an N-terminal domain known as dsRHbd for binding both dsRNA and RNA/DNA hybrid. We find that dsRHbd binds preferentially to RNA/DNA hybrids by over 25-fold and rename it as hybrid binding domain (HBD). The crystal structure of HBD complexed with a 12 bp RNA/DNA hybrid reveals that the RNA strand is recognized by a protein loop, which forms hydrogen bonds with the 2'-OH groups. The DNA interface is highly specific and contains polar residues that interact with the phosphate groups and an aromatic patch that appears selective for binding deoxyriboses. HBD is unique relative to non-sequence-specific dsDNA- and dsRNA-binding domains because it does not use positive dipoles of alpha-helices for nucleic acid binding. Characterization of full-length enzymes with defective HBDs indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1. Similar activity enhancement by small substrate-binding domains linked to the catalytic domain likely occurs in other nucleic acid enzymes.

Indexed as

Amino Acid SequenceAnimalsBase PairingCrystallography, X-RayDNAHumansMiceModels, BiologicalMolecular Sequence DataMutagenesisNucleic Acid HeteroduplexesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRibonuclease HRNADNANucleic Acid HeteroduplexesRibonuclease Hribonuclease HIRNA

Identifiers

PMID18337749
PMCPMC2323259

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.