Evidence map›Paper›PMID 20081200›Full record

ArticleNucleic acids research2010

Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: a combined molecular genetics and bioinformatics study.

Elad Eliahoo, Ron Ben Yosef, Laura Pérez-Cano, Juan Fernández-Recio, Fabian Glaser, Haim Manor

Abstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

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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

12 citing papers in PubMed.

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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

6 authors.

Elad EliahooDepartment of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.
Ron Ben Yosef
Laura Pérez-Cano
Juan Fernández-Recio
Fabian Glaser
Haim Manor

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translin is a single-stranded RNA- and DNA-binding protein, which has been highly conserved in eukaryotes, from man to Schizosaccharomyces pombe. TRAX is a Translin paralog associated with Translin, which has coevolved with it. We generated structural models of the S. pombe Translin (spTranslin), based on the solved 3D structure of the human ortholog. Using several bioinformatics computation tools, we identified in the equatorial part of the protein a putative nucleic acids interaction surface, which includes many polar and positively charged residues, mostly arginines, surrounding a shallow cavity. Experimental verification of the bioinformatics predictions was obtained by assays of nucleic acids binding to amino acid substitution variants made in this region. Bioinformatics combined with yeast two-hybrid assays and proteomic analyses of deletion variants, also identified at the top of the spTranslin structure a region required for interaction with spTRAX, and for spTranslin dimerization. In addition, bioinformatics predicted the presence of a second protein-protein interaction site at the bottom of the spTranslin structure. Similar nucleic acid and protein interaction sites were also predicted for the human Translin. Thus, our results appear to generally apply to the Translin family of proteins, and are expected to contribute to a further elucidation of their functions.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBinding SitesCarrier ProteinsComputational BiologyDNA-Binding ProteinsModels, MolecularMolecular Sequence DataProtein Interaction Domains and MotifsRNA-Binding ProteinsSchizosaccharomyces pombe ProteinsSequence AlignmentTwo-Hybrid System TechniquesCarrier ProteinsDNA-Binding ProteinsRNA-Binding ProteinsSchizosaccharomyces pombe ProteinsTRAX protein, S pombetsn1 protein, S pombeTSN protein, human

Identifiers

PMID20081200
PMCPMC2875027

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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.