EC Number   |
Natural Substrates |
|---|
   3.6.4.B10 | ATP + H2O |
- |
| 3.6.4.B10 | ATP + H2O |
the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress |
| 3.6.4.B10 | more |
ATP-dependent rotational motion of a group II chaperonin |
| 3.6.4.B10 | more |
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 |
| 3.6.4.B10 | more |
indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA |
| 3.6.4.B10 | more |
indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB |
| 3.6.4.B10 | more |
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 |
| 3.6.4.B10 | more |
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 |
| 3.6.4.B10 | more |
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 |
| 3.6.4.B10 | more |
the CCT complex physically interacts with TOR signaling components including TOR, Rheb, and S6K |
