Search results for "non-canonical function"

showing 2 items of 2 documents

Hsp60 Post-translational Modifications: Functional and Pathological Consequences.

2020

Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. The questio…

0301 basic medicinechaperoninnon-canonical functionsReviewMitochondrioncanonical functionsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrychaperonopathies03 medical and health sciences0302 clinical medicineUbiquitinMolecular Bioscienceslcsh:QH301-705.5Molecular Biologybiologycanonical functions chaperonin Hsp60 non-canonical functions post-translation modificationChemistryfungiCitrullinationCell cycleHsp60Cell biology030104 developmental biologylcsh:Biology (General)Mitochondrial permeability transition pore030220 oncology & carcinogenesisChaperone (protein)biology.proteinPhosphorylationHSP60post-translation modificationFrontiers in molecular biosciences
researchProduct

Oligomeric State and Holding Activity of Hsp60

2023

Similar to its bacterial homolog GroEL, Hsp60 in oligomeric conformation is known to work as a folding machine, with the assistance of co-chaperonin Hsp10 and ATP. However, recent results have evidenced that Hsp60 can stabilize aggregation-prone molecules in the absence of Hsp10 and ATP by a different, “holding-like” mechanism. Here, we investigated the relationship between the oligomeric conformation of Hsp60 and its ability to inhibit fibrillization of the Ab40 peptide. The monomeric or tetradecameric form of the protein was isolated, and its effect on beta-amyloid aggregation was separately tested. The structural stability of the two forms of Hsp60 was also investigated using differentia…

amyloid aggregationOrganic ChemistryHsp60; monomer; oligomer; non-canonical function; amyloid aggregationGeneral MedicinemonomerHsp60CatalysisoligomerComputer Science ApplicationsInorganic ChemistryPhysical and Theoretical Chemistrynon-canonical functionMolecular BiologySpectroscopyInternational Journal of Molecular Sciences; Volume 24; Issue 9; Pages: 7847
researchProduct