The 20S Proteasome of Streptomyces coelicolor-Reference-Cited by-同舟云学术

The 20S Proteasome of Streptomyces coelicolor

Published:1998-10-15 Issue:20 Volume:180 Page:5448-5453
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Nagy István¹²,Tamura Tomohiro²,Vanderleyden Jos¹,Baumeister Wolfgang²,De Mot René¹

Affiliation:

1. F. A. Janssens Laboratory of Genetics, Catholic University of Leuven, B-3001 Heverlee, Belgium,1 and

2. Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany2

Abstract

ABSTRACT 20S proteasomes were purified from Streptomyces coelicolor A3(2) and shown to be built from one α-type subunit (PrcA) and one β-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 β 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 ).

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.180.20.5448-5453.1998

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