Evidence map›Paper›PMID 18719385›Full record

ArticleCell cycle (Georgetown, Tex.)2008

Insights into RNA/DNA hybrid recognition and processing by RNase H from the crystal structure of a non-specific enzyme-dsDNA complex.

Pradeep S Pallan, Martin Egli

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Conformation and Pairing Properties of anChemical research in toxicology · 2022
    Article
  7. Review
  8. AON-based degradation of c.151C>T mutantMolecular therapy. Nucleic acids · 2021
    Article
  9. Recent Advances in Oligonucleotide Therapeutics in Oncology.International journal of molecular sciences · 2021
    Review
  10. Review
  11. Article
  12. Novel complex MAD phasing and RNase H structural insights using selenium oligonucleotides.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Pradeep S PallanDepartment of Biochemistry, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232, USA.
Martin Egli
Vanderbilt University · US

Funding

STRUCTURE/FUNCTION OF NUCLEIC ACID THERAPEUTICSR01GM055237 · NIGMS · VANDERBILT UNIVERSITY · PI EGLI, MARTIN · 1997 to 2012
$3.3M
NIGMS NIH HHS R01 GM055237
6 · The paper itself

Abstract

Ribonuclease HI (RNase H) is a member of the nucleotidyl-transferase superfamily and endo-nucleolytically cleaves the RNA portion in RNA/DNA hybrids and removes RNA primers from Okazaki fragments. The enzyme also binds RNA and DNA duplexes but is unable to cleave either. Three-dimensional structures of bacterial and human RNase H catalytic domains bound to RNA/DNA hybrids have revealed the basis for substrate recognition and the mechanism of cleavage. In order to visualize the enzyme's interactions with duplex DNA and to establish the structural differences that afford tighter binding to RNA/DNA hybrids relative to dsDNA, we have determined the crystal structure of Bacillus halodurans RNase H in complex with the B-form DNA duplex [d(CGCGAATTCGCG)](2). The structure demonstrates that the inability of the enzyme to cleave DNA is due to the deviating curvature of the DNA strand relative to the substrate RNA strand and the absence of Mg(2+) at the active site. A subset of amino acids engaged in contacts to RNA 2'-hydroxyl groups in the substrate complex instead bind to bridging or non-bridging phosphodiester oxygens in the complex with dsDNA. Qualitative comparison of the enzyme's interactions with the substrate and inhibitor duplexes is consistent with the reduced binding affinity for the latter and sheds light on determinants of RNase H binding and cleavage specificity.

Indexed as

BacillusCatalytic DomainCrystallizationCrystallography, X-RayDNAHumansNucleic Acid HeteroduplexesRibonuclease HRNADNANucleic Acid HeteroduplexesRibonuclease Hribonuclease HIRNA

Identifiers

PMID18719385
PMCPMC3689302
OpenAlexW2140122662

What OpenQuestion holds

Textmetadata
LicenceTDM
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.