The 20S Proteasome of Streptomyces coelicolor |
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Authors: | Istv n Nagy, Tomohiro Tamura, Jos Vanderleyden, Wolfgang Baumeister, Ren De Mot |
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Affiliation: | István Nagy, Tomohiro Tamura, Jos Vanderleyden, Wolfgang Baumeister, and René De Mot |
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Abstract: | 20S proteasomes were purified from Streptomyces coelicolor A3(2) and shown to be built from one α-type subunit (PrcA) and one β-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 β 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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