Evidence map›Paper›PMID 28238763›Full record

ArticleJournal of molecular biology2017

Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.

Binyuan Zhai, Kevin DuPrez, Tzanko I Doukov, Huan Li, Mengting Huang, Guijun Shang, Jinfeng Ni, Lichuan Gu, Yulong Shen, Li Fan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 10 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

10 authors at 4 institutions in 2 countries.

Binyuan ZhaiState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Kevin DuPrezDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Tzanko I DoukovMacromolecular Crystallography Group, Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA 94309, USA.
Huan LiState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Mengting HuangState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Guijun ShangState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Jinfeng NiState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Lichuan GuState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China.
Yulong ShenState Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Road, Jinan 250100, PR China. Electronic address: yulgshen@sdu.edu.cn.
Li FanDepartment of Biochemistry, University of California, Riverside, CA 92521, USA. Electronic address: lifan@ucr.edu.
Shandong University · CNState Key Laboratory of Microbial TechnologyUniversity of California, Riverside · USStanford Synchrotron Radiation Lightsource · US

Funding

Investigating the role of XPB helicase in DNA nucleotide excision repairR01GM108893 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI FAN, LI · 2015 to 2019
$1.3M
NIGMS NIH HHS R01 GM108893
6 · The paper itself

Abstract

Holliday junction (HJ) is a hallmark intermediate in DNA recombination and must be processed by dissolution (for double HJ) or resolution to ensure genome stability. Although HJ resolvases have been identified in all domains of life, there is a long-standing effort to search in prokaryotes and eukarya for proteins promoting HJ migration. Here, we report the structural and functional characterization of a novel ATPase, Sulfolobus islandicusPilT N-terminal-domain-containing ATPase (SisPINA), encoded by the gene adjacent to the resolvase Hjc coding gene. PINA is conserved in archaea and vital for S. islandicus viability. Purified SisPINA forms hexameric rings in the crystalline state and in solution, similar to the HJ migration helicase RuvB in Gram-negative bacteria. Structural analysis suggests that ATP binding and hydrolysis cause conformational changes in SisPINA to drive branch migration. Further studies reveal that SisPINA interacts with SisHjc and coordinates HJ migration and cleavage.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateCell SurvivalCrystallography, X-RayDNAHolliday Junction ResolvasesHydrolysisModels, MolecularProtein BindingProtein ConformationProtein MultimerizationSulfolobusAdenosine TriphosphatasesAdenosine TriphosphateDNAHolliday Junction ResolvasesarchaeaATPaseDNA recombinational repairHolliday junction migrationSulfolobus islandicus

Identifiers

PMID28238763
PMCPMC5565510
OpenAlexW2590457479

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.