Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits
| Autor: | K, Früh, Y, Yang, D, Arnold, J, Chambers, L, Wu, J B, Waters, T, Spies, P A, Peterson |
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| Rok vydání: | 1992 |
| Předmět: |
Proteasome Endopeptidase Complex
Base Sequence Genes MHC Class II Molecular Sequence Data Gene Expression Membrane Proteins Proteins Exons Major Histocompatibility Complex Viral Matrix Proteins Cysteine Endopeptidases Genes Oligodeoxyribonucleotides Multienzyme Complexes Amino Acid Sequence RNA Messenger Protein Precursors Antigens Viral Protein Processing Post-Translational |
| Zdroj: | The Journal of biological chemistry. 267(31) |
| ISSN: | 0021-9258 |
| Popis: | The finding that two subunits of the proteasome, LMP2 and LMP7, are encoded in the major histocompatibility complex (MHC) has linked the proteasome which represents a major extralysosomal proteolytic system to the processing of intracellular antigens. Here we describe a second form of the human LMP7 cDNA, LMP7-E2, which has been identified during the characterization of novel genes in the MHC. The analysis of the genome organization of LMP7 revealed that LMP7-E1 and LMP7-E2 arise by alternative exon usage. Using specific antibodies against LMP2 and LMP7, we show that they are co-expressed with class I MHC molecules as well as a putative peptide transporter. The polypeptides encoded by LMP7 and LMP2 undergo proteolytic processing when incorporated into proteasomes, and the LMP7 precursor is derived mainly from LMP7-E2. Furthermore, our data suggest that LMP7 and LMP2 are mutually dependent for their incorporation into the proteasomal complex. |
| Databáze: | OpenAIRE |
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