| Literature DB >> 9765579 |
I Nagy1, T Tamura, J Vanderleyden, W Baumeister, R De Mot.
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).Entities:
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Year: 1998 PMID: 9765579 PMCID: PMC107596
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490