Evidence map›Paper›PMID 21572043›Full record

ArticleThe Journal of biological chemistry2011

Characterization of the endonuclease and ATP-dependent flap endo/exonuclease of Dna2.

Barbara K Fortini, Subhash Pokharel, Piotr Polaczek, Lata Balakrishnan, Robert A Bambara, Judith L Campbell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

6 authors at 2 institutions in 1 country.

Barbara K FortiniBraun Laboratories, California Institute of Technology, Pasadena, California 91125, USA.
Subhash Pokharel
Piotr Polaczek
Lata Balakrishnan
Robert A Bambara
Judith L Campbell
California Institute of Technology · USUniversity of Rochester · US

Funding

ENZYMATIC MECHANISMS OF DNA SYNTHESISR01GM024441 · NIGMS · UNIVERSITY OF ROCHESTER · PI BAMBARA, ROBERT A · 1985 to 2011
$3.8M
Enzyme Interactions at the DNA Replication ForkR01GM078666 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 2006 to 2009
$1.5M
NIGMS NIH HHS GM024441NIGMS NIH HHS GM078666NIGMS NIH HHS R01 GM024441NIGMS NIH HHS R01 GM078666
6 · The paper itself

Abstract

Two processes, DNA replication and DNA damage repair, are key to maintaining genomic fidelity. The Dna2 enzyme lies at the heart of both of these processes, acting in conjunction with flap endonuclease 1 and replication protein A in DNA lagging strand replication and with BLM/Sgs1 and MRN/X in double strand break repair. In vitro, Dna2 helicase and flap endo/exonuclease activities require an unblocked 5' single-stranded DNA end to unwind or cleave DNA. In this study we characterize a Dna2 nuclease activity that does not require, and in fact can create, 5' single-stranded DNA ends. Both endonuclease and flap endo/exonuclease are abolished by the Dna2-K677R mutation, implicating the same active site in catalysis. In addition, we define a novel ATP-dependent flap endo/exonuclease activity, which is observed only in the presence of Mn(2+). The endonuclease is blocked by ATP and is thus experimentally distinguishable from the flap endo/exonuclease function. Thus, Dna2 activities resemble those of RecB and AddAB nucleases even more closely than previously appreciated. This work has important implications for understanding the mechanism of action of Dna2 in multiprotein complexes, where dissection of enzymatic activities and cofactor requirements of individual components contributing to orderly and precise execution of multistep replication/repair processes depends on detailed characterization of each individual activity.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid SubstitutionDNA HelicasesDNA RepairDNA ReplicationDNA, Single-StrandedExodeoxyribonucleasesFlap EndonucleasesHumansManganeseMutation, MissenseAdenosine TriphosphatasesAdenosine TriphosphateDNA2 protein, humanDNA HelicasesDNA, Single-StrandedExodeoxyribonucleasesFlap EndonucleasesManganese

Identifiers

PMID21572043
PMCPMC3129157
OpenAlexW2007223305

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.