Evidence map›Paper›PMID 14734815›Full record

ArticleNucleic acids research2004

RNase H2 of Saccharomyces cerevisiae is a complex of three proteins.

Ho-Sang Jeong, Peter S Backlund, Hao-Chia Chen, Alexander A Karavanov, Robert J Crouch

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

51 citing papers in PubMed, 98 citations in OpenAlex.

  1. Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
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  11. Case Report: Novel Compound HeterozygousFrontiers in immunology · 2021
    Article
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  14. Review
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  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ho-Sang JeongLaboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2790, USA.
Peter S Backlund
Hao-Chia Chen
Alexander A Karavanov
Robert J Crouch
National Institutes of Health · US

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
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
THE STRUCTURE AND FUNCTION OF BIOLOGICALLY ACTIVE MOLECULESZ01HD000035 · NICHD · CHILD HEALTH AND HUMAN DEVELOPMENT · PI CHEN, HAO CHIA · 1985 to 2005
–
6 · The paper itself

Abstract

The composition of RNase H2 has been a long-standing problem. Whereas bacterial and archaeal RNases H2 are active as single polypeptides, the Saccharomyces cerevisiae homolog, Rnh2Ap, when expressed in Escherichia coli, fails to produce an active RNase H2. By affinity chromatography purification and identification of polypeptides associated with a tagged S.cerevisiae Rnh2Ap, we obtained a complex of three proteins [Rnh2Ap (Rnh201p), Ydr279p (Rnh202p) and Ylr154p (Rnh203p)] that together are necessary and sufficient for RNase H2 activity [correction]. Deletion of the gene encoding any one of the proteins or mutations in the catalytic site in Rnh2A led to loss of RNase H2 activity. Even when S.cerevisiae RNase H2 is catalytically compromised, it still exhibits a preference for cleavage of the phosphodiester bond on the 5' side of a ribonucleotide-deoxyribonucleotide sequence in substrates mimicking RNA-primed Okazaki fragments or a single ribonucleotide embedded in a duplex DNA. Interestingly, Ydr279p and Ylr154p have homologous proteins only in closely related species. The multisubunit nature of S.cerevisiae RNase H2 may be important both for structural purposes and to provide a means of interacting with other proteins involved in DNA replication/repair and transcription.

Indexed as

Binding SitesCatalysisDNAGene DeletionMutagenesis, Site-DirectedPeptidesProtein Structure, QuaternaryProtein SubunitsRibonuclease HSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificitySubstrate SpecificityUltracentrifugationDNAPeptidesProtein SubunitsRibonuclease Hribonuclease HIribonuclease HIISaccharomyces cerevisiae Proteins

Identifiers

PMID14734815
PMCPMC373335
OpenAlexW1983777834

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.