Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60 [PDF]
Proceedings of the National Academy of Sciences, 1997 Chaperonins are essential for the folding of proteins in bacteria, mitochondria, and chloroplasts. We have functionally characterized the yeast mitochondrial chaperonins hsp60 and hsp10. In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent K d of 0.9 nM and a second molecule of ...
Dubaquié Y, Looser R, Rospert S
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The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. [PDF]
PLoS ONE, 2007 We have previously reported on the discovery of a mitochondrial specific unfolded protein response (mtUPR) in mammalian cells, in which the accumulation of unfolded protein within the mitochondrial matrix results in the transcriptional activation of ...
Tomohisa Horibe, Nicholas J Hoogenraad
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Curcumin affects HSP60 folding activity and levels in neuroblastoma cells [PDF]
, 2020 The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial\u2013mesenchymal transition and ...
Campanella C. +9 more
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Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10 [PDF]
Biochemical Journal, 1994 The refolding of lactate dehydrogenase fully unfolded in 4 M guanidinium chloride was initiated by dilution into assay buffer, and the emergence of active enzyme was recorded. This was performed in the presence of the following chaperonin complexes in the refolding medium: chaperonin-60 (cpn60), cpn60-MgATP, cpn60-Mgp[NH]ppA, cpn60-MgADP in both the ...
Staniforth, RA +3 more
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Oncogenic fusion protein BCR-FGFR1 requires the breakpoint cluster region-mediated oligomerization and chaperonin Hsp90 for activation. [PDF]
, 2020 Mutation and translocation of fibroblast growth factor receptors often lead to aberrant signaling and cancer. This work focuses on the t(8;22)(p11;q11) chromosomal translocation which creates the breakpoint cluster region (BCR) fibroblast growth factor ...
Bisom-Rapp, Ezra W +4 more
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Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles
International Journal of Electrochemical Science, 2021 Heat Shock Protein 60 (HSP60) is a 60 kDa weighting chaperonin that is an evolutionary conserved protein occurring in a wide number of organisms. It can serve as a plasma or blood serum biomarker of serious pathologies including cancer.
Miroslav Pohanka
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The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60 [PDF]
European Journal of Biochemistry, 2001 Mitochondrial chaperonins are necessary for the folding of newly imported and stress‐denatured mitochondrial proteins. The goal of this study was to investigate the structure and function of the mammalian mitochondrial chaperonin system. We present evidence that the 60 kDa chaperonin (mt‐cpn60) exists in solution in dynamic equilibrium between monomers,
G, Levy-Rimler +8 more
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Epitopes of microbial and human heat shock protein 60 and their recognition in myalgic encephalomyelitis. [PDF]
PLoS ONE, 2013 Myalgic encephalomyelitis (ME, also called Chronic Fatigue Syndrome), a common disease with chronic fatigability, cognitive dysfunction and myalgia of unknown etiology, often starts with an infection.
Amal Elfaitouri +8 more
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Crystal Structure of Chaperonin-60 from Paracoccus denitrificans [PDF]
Journal of Molecular Biology, 2001 The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 A resolution by the molecular replacement method. Two heptameric rings of identical subunits of P.cpn60 in adjacent asymmetric units are stacked in a back-to-back manner and form a cylinder, as found in GroEL, cpn60 from Escherichia coli.
Fukami, T. A. +4 more
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Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]
, 1992 Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Guiard, Bernard +6 more
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