ausblenden:
Schlagwörter:
Escherichia-coli; Thermoplasma-acidophilum; Dependent proteases; Sequence-analysis; Rhodococcus; Threonine; Proteins; Subunits; Degradation; Inhibitors.; Microbiology.
Zusammenfassung:
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). [References: 48]
