3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
This is an abbreviated version! For detailed information about chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing), go to the full flat file.
chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain
chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain. The interaction between AML1-ETO and TRiC is transient. HSP70 facilitates the direct association of AML1-ETO with TRiC
TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate
denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate