The 20S proteasome of Streptomyces coelicolor

被引：61

作者：

Nagy, I

Tamura, T

Vanderleyden, J

Baumeister, W

De Mot, R

机构：

[1] Catholic Univ Louvain, FA Janssens Lab Genet, B-3001 Heverlee, Belgium

[2] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

JOURNAL OF BACTERIOLOGY | 1998年 / 180卷 / 20期

关键词：

D O I：

10.1128/JB.180.20.5448-5453.1998

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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).

引用

页码：5448 / 5453

页数：6

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