Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]
PLoS ONE, 2012 Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas +8 more
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Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis [PDF]
Frontiers in Molecular Biosciences, 2018 Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts.
Qian Zhao, Qian Zhao, Cuimin Liu
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P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. [PDF]
PLoS ONE, 2013 Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world today. The causative agent, Plasmodium falciparum, contains an unusual, essential organelle known as the apicoplast.
Anna Vitlin Gruber +6 more
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Chaperonin Abundance Enhances Bacterial Fitness [PDF]
Frontiers in Molecular Biosciences, 2021 The ability of chaperonins to buffer mutations that affect protein folding pathways suggests that their abundance should be evolutionarily advantageous. Here, we investigate the effect of chaperonin overproduction on cellular fitness in Escherichia coli.
C. M. Santosh Kumar +7 more
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Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes [PDF]
BMC Evolutionary Biology, 2010 Background Chaperonin proteins are well known for the critical role they play in protein folding and in disease. However, the recent identification of three diverged chaperonin paralogs associated with the human Bardet-Biedl and McKusick-Kaufman ...
Macario Alberto JL +3 more
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Dynamic complexes in the chaperonin-mediated protein folding cycle [PDF]
Frontiers in Molecular Biosciences, 2016 The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated ...
Celeste Weiss +3 more
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Role of the chaperonin TCP-1 ring complex in protein aggregation and neurodegeneration [PDF]
Frontiers in Molecular NeuroscienceThe chaperonin TCP-1 ring complex (TRiC), also known as chaperonin-containing TCP-1 (CCT) complex, plays a crucial role in protein folding and quality control within the cell.
Vanlalrinchhani Varte +3 more
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Phage Display Selection and In Silico Characterization of Peptides as Potential GroEL Modulators [PDF]
PharmaceuticsBackground/Objectives. Antibiotic resistance is an escalating global health concern, highlighting the need for innovative antibacterial strategies beyond traditional drugs.
Stefania Olla +4 more
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Gene expression asymmetry in Parkinson’s disease: variation of CCT gene expression is correlated with hemisphere specific severity [PDF]
Frontiers in Molecular NeuroscienceParkinson’s disease (PD) symptom onset is typically unilateral, which may be related to molecular differences underlying hemispheric vulnerability. Here we sampled prefrontal cortex bilaterally from people with PD and healthy controls and performed RNA ...
Steven E. Pierce +6 more
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The BBS/CCT chaperonin complex ensures the localization of the adhesion G protein-coupled receptor ADGRV1 to the base of primary cilia [PDF]
Frontiers in Cell and Developmental BiologyPrimary cilia are antenna-like sensory organelles present on almost all eukaryotic cells. Their sensory capacity relies on receptors, in particular G-protein-coupled receptors (GPCRs) which localize to the ciliary membrane.
Joshua Linnert +6 more
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