Abstract
CYTOTOXIC T lymphocytes recognize fragments (peptides) of protein antigens presented by major histocompatibility complex (MHC) class I molecules. In general, the peptides are derived from cytosolic proteins and are then transported to the endoplasmic reticulum where they assemble with the MHC class I heavy chains and β2-microglobulin to form stable and functional class I molecules1–4. The proteases involved in the generation of these peptides are unknown. One candidate is the proteasome, a non-lysosomal proteinase complex abundantly present in the cytosol. Proteasomes have several proteolytically active sites and are complexes of high relative molecular mass (Mr about 600K), consisting of about 20–30 subunits with Mrs between 15 and 30K (refs 5–10). Here we show that at least one of these subunits is encoded by the mouse MHC in the region between the K locus and the MHC class II region, and inducible by interferon-γ. This raises the intriguing possibility that the MHC encodes not only the MHC class I molecules themselves but also proteases involved in the formation of MHC-binding peptides.
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Ortiz-Navarrete, V., Seelig, A., Gernold, M. et al. Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex. Nature 353, 662–664 (1991). https://doi.org/10.1038/353662a0
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DOI: https://doi.org/10.1038/353662a0
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