Evidence map›Paper›PMID 26389736›Full record

ArticleNature chemical biology2015

Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes.

Mahesh K Chand, Neha Nirwan, Fiona M Diffin, Kara van Aelst, Manasi Kulkarni, Christian Pernstich, Mark D Szczelkun, Kayarat Saikrishnan

Abstract read
In one paragraph

Article in Nature chemical biology, 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
–field-weighted citation impact
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.

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  16. Structural basis underlying complex assembly and conformational transition of the type I R-M system.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

8 authors.

Mahesh K ChandDivision of Biology, Indian Institute of Science Education and Research, Pune, India.
Neha NirwanDivision of Biology, Indian Institute of Science Education and Research, Pune, India.
Fiona M DiffinDNA-Protein Interactions Unit, School of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, UK.
Kara van AelstDNA-Protein Interactions Unit, School of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, UK.
Manasi KulkarniDivision of Biology, Indian Institute of Science Education and Research, Pune, India.
Christian PernstichDNA-Protein Interactions Unit, School of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, UK.
Mark D SzczelkunDNA-Protein Interactions Unit, School of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, UK.
Kayarat SaikrishnanDivision of Biology, Indian Institute of Science Education and Research, Pune, India.

Funding

Biotechnology and Biological Sciences Research Council BB/D009715/1Wellcome Trust 084086Wellcome Trust 090207/Z/09/ZWellcome Trust 500048-Z-09-Z
6 · The paper itself

Abstract

Production of endonucleolytic double-strand DNA breaks requires separate strand cleavage events. Although catalytic mechanisms for simple, dimeric endonucleases are known, there are many complex nuclease machines that are poorly understood. Here we studied the single polypeptide Type ISP restriction-modification (RM) enzymes, which cleave random DNA between distant target sites when two enzymes collide after convergent ATP-driven translocation. We report the 2.7-Å resolution X-ray crystal structure of a Type ISP enzyme-DNA complex, revealing that both the helicase-like ATPase and nuclease are located upstream of the direction of translocation, an observation inconsistent with simple nuclease-domain dimerization. Using single-molecule and biochemical techniques, we demonstrate that each ATPase remodels its DNA-protein complex and translocates along DNA without looping it, leading to a collision complex in which the nuclease domains are distal. Sequencing of the products of single cleavage events suggests a previously undescribed endonuclease model, where multiple, stochastic strand-nicking events combine to produce DNA scission.

Indexed as

Adenosine TriphosphateBacterial ProteinsCrystallography, X-RayDNADNA Breaks, Double-StrandedDNA CleavageDNA HelicasesEndonucleasesEscherichia coliGene ExpressionLactococcus lactisModels, MolecularNucleic Acid ConformationProtein ConformationProtein TransportRecombinant ProteinsAdenosine TriphosphateBacterial ProteinsDNADNA HelicasesEndonucleasesRecombinant Proteins

Identifiers

PMID26389736
PMCPMC4636054

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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.