Evidence map›Paper›PMID 10567561›Full record

ArticleMolecular and cellular biology1999

Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease.

J Qiu, Y Qian, P Frank, U Wintersberger, B Shen

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
2.6field-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

77 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Review
  6. Ribonucleotide incorporation into DNA during DNA replication and its consequences.Critical reviews in biochemistry and molecular biology · 2021
    Review
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  8. Article
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  16. Review
  17. Article
  18. Article
  19. The Yin and Yang of R-loop biology.Current opinion in cell biology · 2015
    Review
  20. Article

17 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

5 authors at 1 institution in 2 countries.

J QiuDepartment of Cell and Tumor Biology, City of Hope National Medical Center and Beckman Research Institute, Duarte, California 91010, USA.
Y Qian
P Frank
U Wintersberger
B Shen
City Of Hope National Medical Center · US

Funding

Function Analysis of FEN-1 Nuclease in Genome StabilityR01CA073764 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI BINGHUI SHEN · 2002 to 2026
$7.9M
Role of Nucleases in RNA Primer Removal and MutagenesisR01CA085344 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI SHEN, BINGHUI · 1999 to 2024
$7.7M
STRUCTURE/FUNCTION OF A DNA REPAIR ENDONUCLEASER29CA073764 · NCI · CITY OF HOPE NATIONAL MEDICAL CENTER · PI SHEN, BINGHUI · 1997 to 2001
$264k
NCI NIH HHS CA73764NCI NIH HHS CA85344NCI NIH HHS R01 CA073764NCI NIH HHS R29 CA073764
6 · The paper itself

Abstract

Correct removal of RNA primers of Okazaki fragments during lagging-strand DNA synthesis is a critical process for the maintenance of genome integrity. Disturbance of this process has severe mutagenic consequences and could contribute to the development of cancer. The role of the mammalian nucleases RNase HI and FEN-1 in RNA primer removal has been substantiated by several studies. Recently, RNase H(35), the Saccharomyces cerevisiae homologue of mammalian RNase HI, was identified and its possible role in DNA replication was proposed (P. Frank, C. Braunshofer-Reiter, and U. Wintersberger, FEBS Lett. 421:23-26, 1998). This led to the possibility of moving to the genetically powerful yeast system for studying the homologues of RNase HI and FEN-1, i.e., RNase H(35) and Rad27p, respectively. In this study, we have biochemically defined the substrate specificities and the cooperative as well as independent cleavage mechanisms of S. cerevisiae RNase H(35) and Rad27 nuclease by using Okazaki fragment model substrates. We have also determined the additive and compensatory pathological effects of gene deletion and overexpression of these two enzymes. Furthermore, the mutagenic consequences of the nuclease deficiencies have been analyzed. Based on our findings, we suggest that three alternative RNA primer removal pathways of different efficiencies involve RNase H(35) and Rad27 nucleases in yeast.

Indexed as

Saccharomyces cerevisiae ProteinsBase SequenceCell DivisionDNAEndodeoxyribonucleasesFlap EndonucleasesMolecular Sequence DataMutagenesisRecombinant Fusion ProteinsRibonuclease HRNASaccharomyces cerevisiaeSubstrate SpecificityDNAEndodeoxyribonucleasesFlap EndonucleasesOkazaki fragmentsRAD27 protein, S cerevisiaeRecombinant Fusion ProteinsRibonuclease Hribonuclease HIRNARNA primersSaccharomyces cerevisiae Proteins

Identifiers

PMID10567561
PMCPMC84926
OpenAlexW2157435389

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.