Evidence map›Paper›PMID 27849570›Full record

ArticleMolecular and cellular biology2017

The Werner Syndrome Helicase Coordinates Sequential Strand Displacement and FEN1-Mediated Flap Cleavage during Polymerase δ Elongation.

Baomin Li, Sita Reddy, Lucio Comai

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
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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.

Baomin LiDepartment of Molecular Microbiology and Immunology, Institute for Genetic Medicine, Keck School of Medicine, University of Southern California, Los Angeles, California, USA.
Sita ReddyDepartment of Biochemistry and Molecular Medicine, Institute for Genetic Medicine, Keck School of Medicine, University of Southern California, Los Angeles, California, USA.
Lucio ComaiDepartment of Molecular Microbiology and Immunology, Institute for Genetic Medicine, Keck School of Medicine, University of Southern California, Los Angeles, California, USA comai@med.usc.edu.ORCID http://orcid.org/0000-0003-3109-1841
University of Southern California · US

Funding

Role of the Werner syndrome protein complex in the metabolism of chromosome endsR01AG034156 · NIA · UNIVERSITY OF SOUTHERN CALIFORNIA · PI COMAI, LUCIO · 2010 to 2014
$1.8M
EXTRAMURAL RESEARCH FACILITIES CONTRUCTION PROJECTC06CA062528 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI KEDES, LAURENCE H · 1993 to 1994
–
RESEARCH FACILITIES IMPROVEMENT PROGRAM AND REMODELINGC06RR014514 · NCRR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI KEDES, LAURENCE H · 1999 to 1999
–
NCI NIH HHS C06 CA062528NCRR NIH HHS C06 RR014514NIA NIH HHS R01 AG034156
6 · The paper itself

Abstract

The Werner syndrome protein (WRN) suppresses the loss of telomeres replicated by lagging-strand synthesis by a yet to be defined mechanism. Here, we show that whereas either WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase δ progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 cleavage, a critical step in Okazaki fragment maturation, at these sequences. Helicase activity, as well as the conserved winged-helix (WH) motif and the helicase and RNase D C-terminal (HRDC) domain play important but distinct roles in this process. Remarkably, WRN also influences the formation of FEN1 cleavage products during strand displacement on a nontelomeric substrate, suggesting that WRN recruitment and cooperative interaction with FEN1 during lagging-strand synthesis may serve to regulate sequential strand displacement and flap cleavage at other genomic sites. These findings define a biochemical context for the physiological role of WRN in maintaining genetic stability.

Indexed as

DNA ReplicationAmino Acid MotifsDNADNA Polymerase IIIFlap EndonucleasesHeLa CellsHomeostasisHumansPolymerizationProtein DomainsRecQ HelicasesRepetitive Sequences, Nucleic AcidSubstrate SpecificityTelomereWerner Syndrome HelicaseBloom syndrome proteinDNADNA Polymerase IIIFEN1 protein, humanFlap EndonucleasesRecQ HelicasesWerner Syndrome HelicaseagingDNA helicaseDNA replicationlagging strandlagging-strand synthesisOkazaki fragmenttelomeresWerner syndrome

Identifiers

PMID27849570
PMCPMC5247617
OpenAlexW2553298032

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.