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Journal of Bacteriology, October 1998, p. 5448-5453, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The 20S Proteasome of Streptomyces coelicolor

István Nagy,1,2 Tomohiro Tamura,2 Jos Vanderleyden,1 Wolfgang Baumeister,2 and René De Mot1,*

F. A. Janssens Laboratory of Genetics, Catholic University of Leuven, B-3001 Heverlee, Belgium,1 and Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany2

Received 20 July 1998/Accepted 13 August 1998

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).

* Corresponding author. Mailing address: F. A. Janssens Laboratory of Genetics, Kardinaal Mercierlaan 92, B-3001 Heverlee, Belgium. Phone: 32 16 32 96 81. Fax: 32 16 32 19 66. E-mail: rene.demot{at}agr.kuleuven.ac.be.

Journal of Bacteriology, October 1998, p. 5448-5453, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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