Chaperonins: Nanocarriers with Biotechnological Applications [PDF]
Nanomaterials, 2021 Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins ...
Sergio Pipaón Alcíbar +2 more
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Chaperonin in health and disease [PDF]
Molecular BiomedicineChaperonins, evolutionarily conserved heat shock proteins characterized by subunits of approximately 60 kDa, play indispensable roles in maintaining cellular homeostasis.
Pengfei Xu +8 more
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Friends in need: How chaperonins recognize and remodel proteins that require folding assistance [PDF]
Frontiers in Molecular Biosciences, 2022 Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan +3 more
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A Glimpse Into the Structure and Function of Atypical Type I Chaperonins
Frontiers in Molecular Biosciences, 2018 Chaperonins are a subclass of molecular chaperones that assist cellular proteins to fold and assemble into their native shape. Much work has been done on Type I chaperonins, which has elucidated their elegant mechanism.
Shekhar C Mande
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The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System [PDF]
BiomoleculesHtpB, the chaperonin of the bacterial pathogen L. pneumophila, is found in extracellular locations, even the cytoplasm of host cells. Although chaperonins have an essential cytoplasmic function in protein folding, HtpB exits the cytoplasm to perform ...
Peter Robertson +2 more
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Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins [PDF]
Communications BiologyE. coli chaperonin GroEL forms nano-cages for protein folding. Although the chaperonin-mediated protein folding mechanism is well understood, the role of the conserved glycine and methionine-rich carboxy-terminal residues remains unclear.
C. M. Santosh Kumar +3 more
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Compartmentalization of heme biosynthetic pathways into yeast mitochondria enhances heme production [PDF]
npj Science of FoodSaccharomyces cerevisiae is a generally recognized as safe (GRAS) workhorse strain widely used in the food industry for the cost-effective production of food ingredients. However, the heme production yield in yeast is significantly lower than in bacteria
Jae Yoon Won +4 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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Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis
Biomedicines, 2022 Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes ...
Olga S. Sokolova +7 more
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The Possible Role of the Type I Chaperonins in Human Insulin Self-Association
Life, 2022 Insulin is a hormone that attends to energy metabolism by regulating glucose levels in the bloodstream. It is synthesised within pancreas beta-cells where, before being released into the serum, it is stored in granules as hexamers coordinated by Zn2+ and
Federica Pizzo +6 more
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