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Structure and function of a novel type of ATP-dependent Clp protease.
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- Andersson, Fredrik, 1977 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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- Tryggvesson, Anders, 1975 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
- Sharon, Michal (author)
- show more...
- Diemand, Alexander V (author)
- Classen, Mirjam (author)
- Best, Christoph (author)
- Schmidt, Ronny (author)
- Bukau, Bernd (author)
- Robinson, Carol V (author)
- Witt, Susanne (author)
- Mogk, Axel (author)
- show less...
- (creator_code:org_t)
- 2009
- 2009
- English.
- In: The Journal of biological chemistry. - 0021-9258 .- 1083-351X. ; 284:20, s. 13519-32
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. The main constitutive Clp protease in photosynthetic organisms has evolved into a functionally essential and structurally intricate enzyme. The model Clp protease from the cyanobacterium Synechococcus consists of the HSP100 molecular chaperone ClpC and a mixed proteolytic core comprised of two distinct subunits, ClpP3 and ClpR. We have purified the ClpP3/R complex, the first for a Clp proteolytic core comprised of heterologous subunits. The ClpP3/R complex has unique functional and structural features, consisting of twin heptameric rings each with an identical ClpP3(3)ClpR(4) configuration. As predicted by its lack of an obvious catalytic triad, the ClpR subunit is shown to be proteolytically inactive. Interestingly, extensive modification to ClpR to restore proteolytic activity to this subunit showed that its presence in the core complex is not rate-limiting for the overall proteolytic activity of the ClpCP3/R protease. Altogether, the ClpP3/R complex shows remarkable similarities to the 20 S core of the proteasome, revealing a far greater degree of convergent evolution than previously thought between the development of the Clp protease in photosynthetic organisms and that of the eukaryotic 26 S proteasome.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology (hsv//eng)
Keyword
- Bacterial Proteins
- chemistry
- metabolism
- Catalytic Domain
- physiology
- Endopeptidase Clp
- chemistry
- metabolism
- Heat-Shock Proteins
- chemistry
- metabolism
- Multiprotein Complexes
- chemistry
- metabolism
- Proteasome Endopeptidase Complex
- chemistry
- metabolism
- Protein Structure
- Quaternary
- physiology
- Synechococcus
- enzymology
Publication and Content Type
- ref (subject category)
- art (subject category)
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