Abstract
20S proteasomes were purified from Streptomyces coelicolor A3(2) and shown to be built from one alpha-type subunit (PrcA) and one beta-type subunit (PrcB). The enzyme displayed chymotrypsin-like activity on synthetic substrates and was sensitive to peptide aldehyde and peptide vinyl sulfone inhibitors and to the Streptomyces metabolite lactacystin. Characterization of the structural genes revealed an operon-like gene organization (prcBA) similar to Rhodococcus and Mycobacterium spp. and showed that the beta subunit is encoded with a 53-amino-acid propeptide which is removed during proteasome assembly. The upstream DNA region contains the conserved orf7 and an AAA ATPase gene (arc).
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylcysteine / analogs & derivatives
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Acetylcysteine / pharmacology
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Amino Acid Sequence
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Cloning, Molecular
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Cysteine Endopeptidases / genetics*
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Cysteine Endopeptidases / isolation & purification
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Cysteine Endopeptidases / metabolism
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Cysteine Endopeptidases / ultrastructure
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Cysteine Proteinase Inhibitors / pharmacology
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Genes, Bacterial
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Molecular Sequence Data
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Multienzyme Complexes / genetics*
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Multienzyme Complexes / isolation & purification
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Multienzyme Complexes / metabolism
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Multienzyme Complexes / ultrastructure
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Mycobacterium / enzymology
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Mycobacterium / genetics
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Proteasome Endopeptidase Complex
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Rhodococcus / enzymology
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Rhodococcus / genetics
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Sequence Homology, Amino Acid
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Streptomyces / enzymology
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Streptomyces / genetics*
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Substrate Specificity
Substances
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Cysteine Proteinase Inhibitors
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Multienzyme Complexes
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lactacystin
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Acetylcysteine
Associated data
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GENBANK/AF086832
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GENBANK/AF088800