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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The 20S proteasome of Streptomyces coelicolor.

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).[1]

References

  1. The 20S proteasome of Streptomyces coelicolor. Nagy, I., Tamura, T., Vanderleyden, J., Baumeister, W., De Mot, R. J. Bacteriol. (1998) [Pubmed]
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