Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation
Chaperonins are large, essential, oligomers that facilitate protein folding in chloroplasts, mitochondria, and eubacteria. Plant chloroplast chaperonins are comprised of multiple homologous subunits that exhibit unique properties.
Anna Vitlin Gruber +3 more
doaj +1 more source
Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60
Human mitochondrial chaperonin mHsp60 is essential for mitochondrial function by assisting folding of mitochondrial proteins. Unlike the double-ring bacterial GroEL, mHsp60 exists as a heptameric ring that is unstable and dissociates to subunits.
Joseph Che-Yen Wang, Lingling Chen
doaj +1 more source
Chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial domain of each subunit into the central cavity ...
Kevin M Dalton +2 more
doaj +1 more source
Cryo-EM structure of human mitochondrial HSPD1
Summary: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins.
David P. Klebl +7 more
doaj +1 more source
CCT2 Promotes Prostate Cancer Progression Through EIF3F‐Dependent Stabilization of FASN
ABSTRACT Prostate cancer (PCa) is increasingly recognized to be driven by dysregulated lipid metabolism. Although fatty acid synthase (FASN) is highly expressed in PCa, the mechanisms governing FASN protein stability and its functional integration into oncogenic lipid metabolism remain poorly defined.
Shun Xu +13 more
wiley +1 more source
Targeting WDR12 Unleashes T‐Cell‐Mediated Antitumor Activity in Melanoma by Destabilizing CD276
WDR12 cooperates with the chaperonin subunit CCT7 to maintain CD276 stability on tumor cells, suppressing T‐cell activity and promoting immune escape. SU14813, a small‐molecule WDR12 inhibitor, reduces CD276 stability and relieves CD276‐mediated T‐cell suppression.
Jie Pan +10 more
wiley +1 more source
Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis
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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Streamlining Diagnosis of Bardet–Biedl Syndrome: New Diagnostic Algorithm With Updated Criteria
ABSTRACT Considerable advances have been made in our understanding of Bardet–Biedl syndrome (BBS), particularly in its core clinical features and molecular genetics, warranting an update to the existing diagnostic criteria framework. Using a rigorous, evidence‐based, and consensus‐driven process, a multidisciplinary group of international experts and ...
Jeremy J. Pomeroy +16 more
wiley +1 more source
Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin. [PDF]
Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on ...
Ryo Iizuka +3 more
doaj +1 more source
Proteomic signatures of equine dental tooth tissues in ageing and disease
Abstract Background Ageing and dental disease in horses lead to structural and functional deterioration of dental tissues, yet their molecular signatures remain poorly characterised. Understanding how these processes alter the protein composition of enamel, dentin, cementum and pulp is essential for improving equine oral health and identifying ...
Anders Jensen +8 more
wiley +1 more source

