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 journalArticle

106 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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    Fruh, K., Yang, Y., Arnold, D., Chambers, J., Wu, L., Waters, J. B., Spies, T., & Peterson, P. A. (1992). Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. Journal of Biological Chemistry, 267(31), 22131-22140.