EC Number   |
General Information |
Reference |
|---|
   3.6.4.B10 | evolution |
chaperonin TRiC is evolutionarily conserved |
-, 758115 |
| 3.6.4.B10 | evolution |
chaperonins (CPNs) are subdivided into group I and group II. Group I CPNs are present in bacteria and in the organelles of eukaryotes. Group II CPNs exist in the cytosol of archaea and eukaryotes |
757429 |
| 3.6.4.B10 | evolution |
chaperonins are subdivided into two families, group I and group II chaperonins |
758147 |
| 3.6.4.B10 | evolution |
co-evolution of CCT and the eukaryotic cytoskeleton, overview |
-, 749858 |
| 3.6.4.B10 | evolution |
the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor |
-, 733876 |
| 3.6.4.B10 | evolution |
the enzyme belongs to the archetypal group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex |
734489 |
| 3.6.4.B10 | evolution |
the enzyme belongs to the eukaryotic group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones, e.g. the phosducin-like proteins that enhance TRiC-mediated folding of several substrates. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex |
734489 |
| 3.6.4.B10 | evolution |
the enzyme belongs to the group II chaperonins |
734107 |
| 3.6.4.B10 | evolution |
the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses |
-, 733876 |
| 3.6.4.B10 | evolution |
the enzyme belongs to the group II chaperonins, that play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea |
-, 735091 |
