Evidence map›Paper›PMID 27422335›Full record

ArticlePlasmid

The N-terminus of IntDOT forms hydrophobic interactions during Holliday Junction resolution.

Adam J Kolakowski, Jeffrey F Gardner

Open access · greenAbstract read
In one paragraph

Article in Plasmid. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 96% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Adam J KolakowskiDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, USA. Electronic address: akolako2@illinois.edu.
Jeffrey F GardnerDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, USA.
University of Illinois Urbana-Champaign · US

Funding

SITE-SPECIFIC RECOMBINATIONR01GM028717 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GARDNER, JEFFREY F · 1985 to 2013
$4.0M
NIGMS NIH HHS R01 GM028717
6 · The paper itself

Abstract

DOT Integrase (IntDOT) is a member of the tyrosine recombinase family. It catalyzes the integration and excision reactions of an integrative and conjugative element (ICE) called CTnDOT. Like other tyrosine recombinases, the integration reaction proceeds by two sets of strand exchanges between the attDOT site on CTnDOT and an attB site in the host chromosome. The strand exchanges occur seven bases apart and define an overlap region. After the first strand exchanges a Holliday Junction (HJ) intermediate is formed. Previous work showed that a valine (V95) in a predicted alpha helix in the N-terminus of IntDOT is required for resolution of HJs to substrates and products. We have identified two additional hydrophobic residues in the helix (A92 and F99) that are involved in resolution of HJs. IntDOT proteins with substitutions at these residues form aberrant complexes in an electrophoretic mobility shift assay. We propose that these three residues participate in hydrophobic interactions that are involved in forming higher-order complexes and resolution of HJs.

Indexed as

Protein Interaction Domains and MotifsBacteroidesCatalysisConjugation, GeneticDNA, CruciformHydrophobic and Hydrophilic InteractionsIntegrasesMutationProtein BindingDNA, CruciformIntegrasesConjugative transposonCTnDOTIntegraseIntegrative and conjugative element

Identifiers

PMID27422335
PMCPMC5121019
OpenAlexW2463290128

What OpenQuestion holds

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LicenceTDM
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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.