Results 161 to 170 of about 171,782 (185)
Some of the next articles are maybe not open access.
Clp Protease Complexes and Their Diversity in Chloroplasts
Planta, 1998The Clp proteases represent a large, ancient ATP-dependent protease family which in higher plants is known to be located in chloroplasts. The soluble, presumably multisubunit, enzyme of the organelle stroma is of dual genetic origin. It consists of a nuclear-encoded, regulatory subunit ClpC, which is an ATPase, and a plastid-encoded proteolytic subunit
Anna Sokolenko +2 more
exaly +3 more sources
Organization, Function and Substrates of the Essential Clp Protease System in Plastids
Biochimica Et Biophysica Acta - Bioenergetics, 2015 Intra-plastid proteolysis is essential in plastid biogenesis, differentiation and plastid protein homeostasis (proteostasis). We provide a comprehensive review of the Clp protease system present in all plastid types and we draw lessons from structural and functional information of bacterial Clp systems.
Klaas J van Wijk, Kenji Nishimura
exaly +3 more sources
Adapting the Machine: Adaptor Proteins for Hsp100/Clp and AAA+ Proteases
Nature Reviews Microbiology, 2009Members of the AAA+ protein superfamily contribute to many diverse aspects of protein homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic machines in bacteria, AAA+ proteins play a crucial part not only in general protein quality control but also in the regulation of developmental programmes, through the controlled ...
David A. Dougan +2 more
exaly +3 more sources
Effect of Clp Protease From Corynebacterium glutamicum on Heterologous Protein Expression
Protein Expression and Purification, 2022The protease present in a host may reduce the yield and biological activity of heterologous proteins. In this study, we used protease overexpression and deletion strategies to examine the effect of the Clp protease system in Corynebacterium glutamicum on the recombinant protein and to produce a highly efficient heterologous protein expression host.
Zihao Zhao, Xiuxia Liu, Yankun Yang
exaly +3 more sources
ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli
Biochemical Society Transactions, 1991Summary Clp protease is a high relative molecular mass, ATP-dependent protease found in the cytoplasm of Escherichia coli. Clp protease is composed of two protein components, Clp A, which has ATPase activity, and Clp P, which has the proteolytic active site and is activated by Clp A in the presence of ATP.
openaire +2 more sources
The Clp Chaperones and Proteases of the Human Malaria Parasite Plasmodium falciparum
Journal of Molecular Biology, 2010The Clp chaperones and proteases play an important role in protein homeostasis in the cell. They are highly conserved across prokaryotes and found also in the mitochondria of eukaryotes and the chloroplasts of plants. They function mainly in the disaggregation, unfolding and degradation of native as well as misfolded proteins.
Majida, El Bakkouri +12 more
openaire +2 more sources
Uvr Motifs Regulate the Chloroplast Clp Chaperone–Protease System
Trends in Plant ScienceChloroplast proteostasis relies on diverse proteases, including the essential Clp chaperone-protease system. Two chloroplast ClpC AAA+ chaperones and the plant-specific adaptor ClpF contain an Uvr motif with predicted coiled-coiled structures implicated in protein-protein interactions.
Marissa Y Annis +2 more
exaly +3 more sources
ATP-Dependent association between subunits of Clp protease in pea chloroplasts
Planta, 2001The chloroplast ATP-dependent Clp protease (EC 3.4.21.92) is composed of the proteolytic subunit ClpP and the regulatory ATPase, ClpC. Although both subunits are found in the stroma, the interaction between the two is dynamic. When immunoprecipitation with antibodies against ClpC was performed on stroma from dark-adapted pea (Pisum sativum L.
T, Halperin, O, Ostersetzer, Z, Adam
openaire +2 more sources
Biochemical Journal, 2012
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. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the Hsp100/ClpC chaperone partnering a proteolytic core of catalytic ...
Tryggvesson, A. +4 more
openaire +4 more sources
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. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the Hsp100/ClpC chaperone partnering a proteolytic core of catalytic ...
Tryggvesson, A. +4 more
openaire +4 more sources