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  The first characterization of a eubacterial proteasome - the 2os complex of rhodococcus

Tamura, T., Nagy, I., Lupas, A., Lottspeich, F., Cejka, Z., Schoofs, G., et al. (1995). The first characterization of a eubacterial proteasome - the 2os complex of rhodococcus. Current Biology, 5(7), 766-774.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-732F-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7330-8
Genre: Journal Article

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Tamura, T., Author
Nagy, I.1, Author              
Lupas, A.1, Author              
Lottspeich, F.1, Author              
Cejka, Z., Author
Schoofs, G., Author
Tanaka, K., Author
Demot, R., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Molecular-weight proteases; Sodium dodecyl-sulfate; Multicatalytic proteinase; Thermoplasma-acidophilum; Gel-electrophoresis; Ubiquitin; Identification.; Experimental biology & medicine.
 Abstract: Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation. The proteolytic core of the complex is formed by the 20S proteasome, a cylinder-shaped particle that in archaebacteria contains two different subunits (alpha and beta) and in eukaryotes contains fourteen different subunits (seven of the alpha-type and seven of the beta-type). Results: We have purified a 20S proteasome complex from the nocardioform actinomycete Rhodococcus sp. strain NI86/21. The complex has an apparent relative molecular mass of 690 kD, and efficiently degrades the chymotryptic substrate Suc-Leu-Leu-Val-Tyr-AMC in the presence or absence of 0.05 % SDS. Purified preparations reveal the existence of four subunits, two of the alpha-type and two of the beta-type, the genes for which we have cloned and sequenced. Electron micrographs show that the complex has the four-ringed, cylinder-shaped appearance typical of proteasomes. Conclusions: The recent description of the first eubacterial ubiquitin, and our discovery of a eubacterial proteasome show that the ubiquitin pathway of protein degradation is ancestral and common to all forms of life. [References: 41]

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 Dates: 1995-07-01
 Publication Status: Published in print
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 Identifiers: eDoc: 318549
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Title: Current Biology
Source Genre: Journal
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Pages: - Volume / Issue: 5 (7) Sequence Number: - Start / End Page: 766 - 774 Identifier: -