Eubacterial proteasomes |
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Authors: | Lupas Andrei Zühl Frank Tamura Tomohiro Wolf Stefan Nagy István De Mot René Baumeister Wolfgang |
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Institution: | (1) Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany;(2) F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, B-3001 Heverlee, Belgium |
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Abstract: | Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure. |
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Keywords: | proteasome HslVU Clp multicatalytic protease ATP-dependent proteolysis Rhodococcus erythropolis |
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