Abstract
During the search for genes coding for the mouse α and β subunits of the antigen-specific receptor of mouse T cells we encountered a third gene, subsequently designated γ1. This gene has many properties in common with the α and β genes1,2; somatic assembly from gene segments that resemble the gene segments for immunoglobulin variable (V), joining (J) and constant (C) regions; rearrangement and expression in T cells and not in B cells; low but distinct sequence homology to immunoglobulin V, J and C regions; other sequences that are reminiscent of the transmembrane and intracytoplasmic regions of integral membrane proteins; and a cysteine residue at the position expected for a disulphide bond linking two subunits of a dimeric membrane protein. Despite these similarities the γ gene also shows some interesting unique features. These include a relatively limited repertoire of the germ-line gene segments2–5, more pronounced expression at the RNA level in immature T cells such as fetal thymocytes6–8 and an apparent absence of in-frame RNA in some functional, αβ heterodimer-bearing T cells or cultured T clones and hybridomas9,10. To understand the function of the putative y protein it is essential to define the cell population that expresses this protein. To this end we produced a fusion protein composed of Escherichia coli β-galactosidase and the γ-chain (hereafter referred to a β-gal-γ) using the phage expression vector λgt11 (ref. 11) and raised rabbit antisera against the γ determinants. Using the purified anti-γ antibody we detected a polypeptide chain of relative molecular mass 35,000 (Mr35K) on the surface of 16-day old fetal thymocytes. The γ-chain is linked by a disulphide bridge to another component of 45K. No such heterodimer was detected on the surface of a cytotoxic T lymphocyte (CTL) clone 2C12 from which an in-phase γ cDNA clone was originally isolated.
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Nakanishi, N., Maeda, K., Ito, Ki. et al. Tγ protein is expressed on murine fetal thymocytes as a disulphide-linked heterodimer. Nature 325, 720–723 (1987). https://doi.org/10.1038/325720a0
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DOI: https://doi.org/10.1038/325720a0
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