Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits

K. Fruh, Y. Yang, D. Arnold, J. Chambers, L. Wu, J. B. Waters, T. Spies, P. A. Peterson

Research output: Contribution to journalArticlepeer-review

108 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)22131-22140
Number of pages10
JournalJournal of Biological Chemistry
Volume267
Issue number31
StatePublished - Jan 1 1992

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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