Evidence map›Paper›PMID 26384418›Full record

ArticleNucleic acids research2015

The Bacteroides sp. 3_1_23 Pif1 protein is a multifunctional helicase.

Na-Nv Liu, Xiao-Lei Duan, Xia Ai, Yan-Tao Yang, Ming Li, Shuo-Xing Dou, Stephane Rety, Eric Deprez, Xu-Guang Xi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. NAL1 forms a molecular cage to regulate FZP phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

9 authors at 4 institutions in 2 countries.

Na-Nv LiuCollege of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Xiao-Lei DuanCollege of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Xia AiCollege of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Yan-Tao YangCollege of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Ming LiCAS Key Laboratory of Soft Matter Physics, International Associated Laboratory of CNRS-Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Shuo-Xing DouCAS Key Laboratory of Soft Matter Physics, International Associated Laboratory of CNRS-Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Stephane RetyInstitut de Biochimie et Chimie des protéines, CNRS UMR5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
Eric DeprezLaboratoire de Biologie et Pharmacologie Appliquée, ENS Cachan, CNRS UMR8113, IDA FR3242, F-94235 Cachan, France.
Xu-Guang XiCollege of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China Laboratoire de Biologie et Pharmacologie Appliquée, ENS Cachan, CNRS UMR8113, IDA FR3242, F-94235 Cachan, France xxi01@ens-cachan.fr.
Northwest A&F University · CNCentre National de la Recherche Scientifique · FRChinese Academy of Sciences · CNInstitut de Biologie et de Chimie des Protéines · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ScPif1 DNA helicase is the prototypical member of a 5'-to-3' helicase superfamily conserved from bacteria to human and plays various roles in the maintenance of genomic homeostasis. While many studies have been performed with eukaryotic Pif1 helicases, including yeast and human Pif1 proteins, the potential functions and biochemical properties of prokaryotic Pif1 helicases remain largely unknown. Here, we report the expression, purification and biochemical analysis of Pif1 helicase from Bacteroides sp. 3_1_23 (BsPif1). BsPif1 binds to a large panel of DNA substrates and, in particular, efficiently unwinds partial duplex DNAs with 5'-overhang, fork-like substrates, D-loop and flap-like substrates, suggesting that BsPif1 may act at stalled DNA replication forks and enhance Okazaki fragment maturation. Like its eukaryotic homologues, BsPif1 resolves R-loop structures and unwinds DNA-RNA hybrids. Furthermore, BsPif1 efficiently unfolds G-quadruplexes and disrupts nucleoprotein complexes. Altogether, these results highlight that prokaryotic Pif1 helicases may resolve common issues that arise during DNA transactions. Interestingly, we found that BsPif1 is different from yeast Pif1, but resembles more human Pif1 with regard to substrate specificity, helicase activity and mode of action. These findings are discussed in the context of the possible functions of prokaryotic Pif1 helicases in vivo.

Indexed as

Bacterial ProteinsBacteroidesDNADNA HelicasesG-QuadruplexesSubstrate SpecificityBacterial ProteinsDNADNA Helicases

Identifiers

PMID26384418
PMCPMC4605326
OpenAlexW2134565464

What OpenQuestion holds

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Registered trials

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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.