The 20S proteasome of Streptomyces coelicolor.
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ABSTRACT:
SUBMITTER: Nagy I
PROVIDER: S-EPMC107596 | biostudies-literature | 1998 Oct
REPOSITORIES: biostudies-literature
Publications
The 20S proteasome of Streptomyces coelicolor.
Nagy I I Tamura T T Vanderleyden J J Baumeister W W De Mot R R
Journal of bacteriology 19981001 20
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 t ...[more]
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