Evidence map›Paper›PMID 26717024›Full record

ArticleDNA repair2016

RECQL5 has unique strand annealing properties relative to the other human RecQ helicase proteins.

Prabhat Khadka, Deborah L Croteau, Vilhelm A Bohr

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  5. RECQL5 at theFrontiers in cell and developmental biology · 2020
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
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

3 authors at 1 institution in 1 country.

Prabhat KhadkaLaboratory of Molecular Gerontology, National Institute on Aging, Intramural Research Program (NIA IRP), Biomedical Research Center, Baltimore, MD 21224, USA.
Deborah L CroteauLaboratory of Molecular Gerontology, National Institute on Aging, Intramural Research Program (NIA IRP), Biomedical Research Center, Baltimore, MD 21224, USA.
Vilhelm A BohrLaboratory of Molecular Gerontology, National Institute on Aging, Intramural Research Program (NIA IRP), Biomedical Research Center, Baltimore, MD 21224, USA. Electronic address: vbohr@nih.gov.
National Institute on Aging · US

Funding

Function of RecQ helicases in genome stabilityZIAAG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT · 2009 to 2025
$13.1M
The Function of Werner Syndrome ProteinZIAAG000721 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$7.7M
Function of RecQ helicases in genome stabilityZ01AG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 1993 to 2008
$2.9M
Intramural NIH HHS Z01 AG000726
6 · The paper itself

Abstract

The RecQ helicases play important roles in genome maintenance and DNA metabolism (replication, recombination, repair, and transcription). Five different homologs are present in humans, three of which are implicated in accelerated aging genetic disorders: Rothmund Thomson (RECQL4), Werner (WRN), and Bloom (BLM) syndromes. While the DNA helicase activities of the 5 human RecQ helicases have been extensively characterized, much less is known about their DNA double strand annealing activities. Strand annealing is an important integral enzymatic activity in DNA metabolism, including DNA repair. Here, we have characterized the strand annealing activities of all five human RecQ helicase proteins and compared them. Interestingly, the relative strand annealing activities of the five RecQ proteins are not directly (inversely) related to their helicase activities. RECQL5 possesses relatively strong annealing activity on long or small duplexed substrates compared to the other RecQs. Additionally, the strand annealing activity of RECQL5 is not inhibited by the presence of ATP, unlike the other RecQs. We also show that RECQL5 efficiently catalyzes annealing of RNA to DNA in vitro in the presence or absence of ATP, revealing a possible new function for RECQL5. Additionally, we investigate how different known RecQ interacting proteins, RPA, Ku, FEN1 and RAD51, regulate their strand annealing activity. Collectively, we find that the human RecQ proteins possess differential DNA double strand annealing activities and we speculate on their individual roles in DNA repair. This insight is important in view of the many cellular DNA metabolic actions of the RecQ proteins and elucidates their unique functions in the cell.

Indexed as

DNA RepairAdenosine TriphosphateAntigens, NuclearDNADNA-Binding ProteinsFlap EndonucleasesHumansKu AutoantigenRad51 RecombinaseRecQ HelicasesSubstrate SpecificityAdenosine TriphosphateAntigens, NuclearDNADNA-Binding ProteinsFEN1 protein, humanFlap EndonucleasesKu AutoantigenRAD51 protein, humanRad51 RecombinaseRecQ HelicasesRECQL5 protein, humanXrcc6 protein, humanAgingDNA–DNA hybridDNA repairRecQ helicaseRNA–DNA hybridStrand annealing

Identifiers

PMID26717024
PMCPMC5903426
OpenAlexW2183110188

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.