Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-10

AUTHORS

Coleen K. Martinez, John J. Monaco

ABSTRACT

THE class II region of the major histocompatibility complex (MHC) contains genes encoding at least two subunits of a large, intracellular protein complex (the low molecular mass polypeptide, or LMP, complex)1–3. This complex is biochemically similar to the proteasome, an abundant and well conserved protein complex having multiple proteolytic activities. Here we report the isolation of a complementary DNA corresponding to one of the subunits of the LMP complex, LMP-2. The protein predicted from this cDNA sequence closely matches the amino-terminal peptide sequence of a rat proteasome subunit, confirming that the proteasome and the LMP complex share polypeptide subunits. The LMP-2 gene is tightly linked to HAM1, a gene thought to be required for translocating peptide fragments of endogenous antigens into the endoplasmic reticulum for association with MHC class I molecules4. These observations suggest that the LMP complex may be responsible for generating peptides from cytoplas-mic antigen during antigen processing. More... »

PAGES

664-667

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/353664a0

DOI

http://dx.doi.org/10.1038/353664a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047893865

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1681432


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