ArticleBiochemical and biophysical research communications2010
Analysis of nucleic acid binding by a recombinant translin-trax complex.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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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.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Combined protein- and nucleic acid-level effects of rs1143679 (R77H), a lupus-predisposing variant within ITGAM.Human molecular genetics · 2014Article
- Characterization of a plant (rice) translin and its comparative analysis with human translin.Planta · 2014Article
- Molecular evolution of translin superfamily proteins within the genomes of eubacteria, archaea and eukaryotes.Journal of molecular evolution · 2012Article
- Identification of nucleic acid binding sites on translin-associated factor X (TRAX) protein.PloS one · 2012Article
- Low-resolution structure of Drosophila translin.FEBS open bio · 2012Article
- Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex.Nature structural & molecular biology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Translin is a highly conserved mammalian RNA and DNA-binding protein involved in DNA recombination and RNA trafficking. Crystal structures of mouse and human translin have been solved, but do not provide information about nucleic acid binding or recognition. Translin has a partner protein, translin-associated factor x (trax), which is believed to regulate translin's subcellular locale and affinity for certain RNA and DNA sequences. Here we present a comparative study of recombinant translin and translin-trax complex binding to specific RNA and DNA sequences. It was observed that translin preferentially binds to G-rich RNA sequences whereas translin-trax preferentially binds G-rich DNA sequences. Translin can bind mRNA sequences with sub-micromolar K(d) values, and the complex with trax can bind G-rich DNA with similar affinity. We conclude that trax acts to regulate translin's RNA and DNA binding affinities as part of a cellular RNA trafficking mechanism.
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Registered trials
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