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  • Title: The 20S proteasome of Streptomyces coelicolor.
    Author: Nagy I, Tamura T, Vanderleyden J, Baumeister W, De Mot R.
    Journal: J Bacteriol; 1998 Oct; 180(20):5448-53. PubMed ID: 9765579.
    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).
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