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Journal Article

The 20s proteasome of streptomyces coelicolor

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Nagy, I., Tamura, T., Vanderleyden, J., Baumeister, W., & Demot, R. (1998). The 20s proteasome of streptomyces coelicolor. Journal of Bacteriology, 180(20), 5448-5453.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-71EF-C
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). [References: 48]