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Updated: Aug 12, 2026

Generating De Novo Antigen-specific Human T Cell Receptors by Retroviral Transduction of Centric Hemichain
Published on: October 25, 2016
SMAR1, a novel, alternatively spliced gene product, binds the Scaffold/Matrix-associated region at the T cell
S Chattopadhyay1, R Kaul, A Charest
1National Center for Cell Science, Ganeshkhind, Maharastra, Pune-411007, India.
Abstract:
Rearrangement and expression of the T cell receptor beta gene are critical events for early T lymphocyte development. To characterize cis-regulatory elements and their associated trans-factors that mediate these events, we have previously identified a nuclear matrix/scaffold-associated region, referred to as MARbeta, 400 bp upstream of the Ebeta enhancer. Electrophoretic mobility shift assay showed that two known MAR-binding proteins, SATB1 and Cux, bind MARbeta. In this article, we report the identification of a novel MAR-binding protein, named SMAR1, that also binds MARbeta. SMAR1 shares homology with SATB1 and Cux in the MAR-binding domain/Cut repeat and also with the tetramerization domain of a B cell-specific MAR-binding protein, Bright. The binding of GST-SMAR1 fusion protein to MARbeta is inhibited by the presence of an excess amount of MAR-containing DNA from the immunoglobulin kappa locus. Smar1 transcripts are most abundant in the thymus and are alternatively spliced. The smar1 gene maps to the distal portion of mouse chromosome 8 at a distance of 111.8 cM.
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