Evidence map›Paper›PMID 31017574›Full record

ArticleeLife2019

Novel RNA and DNA strand exchange activity of the PALB2 DNA binding domain and its critical role for DNA repair in cells.

Jaigeeth Deveryshetty, Thibaut Peterlini, Mikhail Ryzhikov, Nadine Brahiti, Graham Dellaire, Jean-Yves Masson, Sergey Korolev

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 25 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Jaigeeth DeveryshettyEdward A Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, United States.
Thibaut PeterliniGenome Stability Laboratory, CHU de Québec-Université Laval, Oncology Division, Laval University Cancer Research Center, Québec City, Canada.
Mikhail RyzhikovEdward A Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, United States.
Nadine BrahitiGenome Stability Laboratory, CHU de Québec-Université Laval, Oncology Division, Laval University Cancer Research Center, Québec City, Canada.
Graham DellaireDepartment of Pathology, Dalhousie University, Halifax, Canada.ORCID 0000-0002-3466-6316
Jean-Yves MassonGenome Stability Laboratory, CHU de Québec-Université Laval, Oncology Division, Laval University Cancer Research Center, Québec City, Canada.
Sergey KorolevEdward A Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, United States.ORCID 0000-0001-9313-7126
Saint Louis University · USUniversité Laval · CADalhousie University · CA

Funding

Structure-function of recombination/replication mediatorR01GM073837 · NIGMS · SAINT LOUIS UNIVERSITY · PI KOROLEV, SERGEY · 2006 to 2010
$1.4M
NIGMS NIH HHS R01 GM073837
6 · The paper itself

Abstract

BReast Cancer Associated proteins 1 and 2 (BRCA1, -2) and Partner and Localizer of BRCA2 (PALB2) protein are tumour suppressors linked to a spectrum of malignancies, including breast cancer and Fanconi anemia. PALB2 coordinates functions of BRCA1 and BRCA2 during homology-directed repair (HDR) and interacts with several chromatin proteins. In addition to protein scaffold function, PALB2 binds DNA. The functional role of this interaction is poorly understood. We identified a major DNA-binding site of PALB2, mutations in which reduce RAD51 foci formation and the overall HDR efficiency in cells by 50%. PALB2 N-terminal DNA-binding domain (N-DBD) stimulates the function of RAD51 recombinase. Surprisingly, it possesses the strand exchange activity without RAD51. Moreover, N-DBD stimulates the inverse strand exchange and can use DNA and RNA substrates. Our data reveal a versatile DNA interaction property of PALB2 and demonstrate a critical role of PALB2 DNA binding for chromosome repair in cells.

Indexed as

DNA RepairRecombination, GeneticBinding SitesCell LineDNADNA-Binding ProteinsFanconi Anemia Complementation Group N ProteinHumansRNADNADNA-Binding ProteinsFanconi Anemia Complementation Group N ProteinPALB2 protein, humanRNAbiochemistrycancer biologychemical biologyDNA recombinationDNA repairE. colihumanprotein-DNA interactiontumor supressor

Identifiers

PMID31017574
PMCPMC6533086
OpenAlexW2941251866

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.