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Structure and Function of a Novel Type of ATP-dependent Clp Protease

Andersson, Fredrik I.; Tryggvesson, Anders; Sharon, Michal; Diemand, Alexander V.; Classen, Mirjam; Best, Christoph; Schmidt, Ronny; Schelin, Jenny LU ; Stanne, Tara M. and Bukau, Bernd, et al. (2009) In Journal of Biological Chemistry 284(20). p.13519-13532
Abstract
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... (More)
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. (Less)
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Journal of Biological Chemistry
volume
284
issue
20
pages
13519 - 13532
publisher
ASBMB
external identifiers
  • wos:000265877300029
  • scopus:67649413592
ISSN
1083-351X
DOI
10.1074/jbc.M809588200
language
English
LU publication?
yes
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c30d6653-c8a2-453d-b8de-23ab407eda60 (old id 1425968)
date added to LUP
2009-06-26 14:25:56
date last changed
2017-09-17 04:49:51
@article{c30d6653-c8a2-453d-b8de-23ab407eda60,
  abstract     = {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.},
  author       = {Andersson, Fredrik I. and Tryggvesson, Anders and Sharon, Michal and Diemand, Alexander V. and Classen, Mirjam and Best, Christoph and Schmidt, Ronny and Schelin, Jenny and Stanne, Tara M. and Bukau, Bernd and Robinson, Carol V. and Witt, Susanne and Mogk, Axel and Clarke, Adrian K.},
  issn         = {1083-351X},
  language     = {eng},
  number       = {20},
  pages        = {13519--13532},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Structure and Function of a Novel Type of ATP-dependent Clp Protease},
  url          = {http://dx.doi.org/10.1074/jbc.M809588200},
  volume       = {284},
  year         = {2009},
}