Ontology type: schema:ScholarlyArticle
1993-09
AUTHORSJames Driscoll, Michael G. Brown, Daniel Finley, John J. Monaco
ABSTRACTPROTEASOMES are highly conserved macromolecular structures which function as endopeptidases1–3. They are found in the cyto-plasm and nucleus of eukaryotic tissues and consist of at least 14 non-identical subunits with molecular masses ranging from ∼20 to 32K. Proteasomes are essential in the selective degradation of ubiquitinated and certain non-ubiquitinated proteins, acting as the proteolytic core of an energy-dependent 26S (1,500K) proteolytic complex. Two proteasome subunits, LMP2 and LMP7 (refs 4–7), are encoded within the major histocompatibility complex (MHC), implicating proteasomes in antigen processing8,9. Here we deter-mine the function of these two MHC-linked subunits by comparing the proteolytic activities of purified proteasomes containing (LMP+) or lacking (LMP−) these components. We find that pro-teasomes of both types have endopeptidase activity against sub-strates bearing hydrophobic, basic or acidic residues immediately preceding the cleavage site (the PI position) and at sites following asparagine, glycine and proline residues. The activity of LMP+ proteasomes is much higher than that of LMP− proteasomes against substrates with hydrophobic, basic or asparagine residues at PI, whereas their activities are comparable when acidic and glycine residues are present at PI. The MHC-linked LMP2 and LMP7 subunits therefore function to amplify specific endopeptid-ase activities of the proteasome. More... »
PAGES262-264
http://scigraph.springernature.com/pub.10.1038/365262a0
DOIhttp://dx.doi.org/10.1038/365262a0
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/8371781
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