Evidence map›Paper›PMID 28039325›Full record

ArticleNucleic acids research2017

Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA.

Giedre Tamulaitiene, Virginija Jovaisaite, Gintautas Tamulaitis, Inga Songailiene, Elena Manakova, Mindaugas Zaremba, Saulius Grazulis, Shuang-Yong Xu, Virginijus Siksnys

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. A short history of Auto-Rickshaw.Acta crystallographica. Section D, Structural biology · 2026
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  6. Predicting Hot Spot Residues at Protein-DNA Binding Interfaces Based on Sequence Information.Interdisciplinary sciences, computational life sciences · 2021
    Article
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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 2 institutions in 2 countries.

Giedre TamulaitieneInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Virginija JovaisaiteInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Gintautas TamulaitisInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Inga SongailieneInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Elena ManakovaInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Mindaugas ZarembaInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Saulius GrazulisInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Shuang-Yong XuNew England Biolabs, Inc. 240 County Road, Ipswich, MA 01938, USA.
Virginijus SiksnysInstitute of Biotechnology, Vilnius University, Sauletekio al. 7, LT-10257 Vilnius, Lithuania.
Vilnius University · LTNew England Biolabs (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although all Type II restriction endonucleases catalyze phosphodiester bond hydrolysis within or close to their DNA target sites, they form different oligomeric assemblies ranging from monomers, dimers, tetramers to higher order oligomers to generate a double strand break in DNA. Type IIP restriction endonuclease AgeI recognizes a palindromic sequence 5΄-A/CCGGT-3΄ and cuts it ('/' denotes the cleavage site) producing staggered DNA ends. Here, we present crystal structures of AgeI in apo and DNA-bound forms. The structure of AgeI is similar to the restriction enzymes that share in their target sites a conserved CCGG tetranucleotide and a cleavage pattern. Structure analysis and biochemical data indicate, that AgeI is a monomer in the apo-form both in the crystal and in solution, however, it binds and cleaves the palindromic target site as a dimer. DNA cleavage mechanism of AgeI is novel among Type IIP restriction endonucleases.

Indexed as

DNA CleavageApoenzymesBase PairingCatalytic DomainDeoxyribonucleases, Type II Site-SpecificDNAModels, MolecularProtein BindingProtein MultimerizationApoenzymesDeoxyribonucleases, Type II Site-SpecificDNA

Identifiers

PMID28039325
PMCPMC5389614
OpenAlexW2562170907

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.