EC Number   |
General Information |
Reference |
|---|
   5.6.1.7 | evolution |
GroEL belongs to the heat shock family of proteins (HSPs), also known as Hsp60 or Group I chaperonin |
-, 733223 |
| 5.6.1.7 | evolution |
the bacterial chaperonin GroEL, with its lid-like cofactor GroES, is the archetypical member of the class of protein folding machines. GroEL belongs to the chaperonins of group I, which are found in bacteria as well as in mitochondria and chloroplasts, the eukaryotic organelles that descend from bacterial endosymbionts |
735322 |
| 5.6.1.7 | evolution |
the chaperonins are a family of molecular chaperones present in all three kingdoms of life. They are classified into group I and group II. Group I consists of the bacterial variants (GroEL) and the eukaryotic ones from mitochondria and chloroplasts (Hsp60). Both groups assemble into a dual ring structure, with each ring providing a protective folding chamber for nascent and denatured proteins |
733876 |
| 5.6.1.7 | malfunction |
a wider range of newly synthesized proteins aggregated upon rapid loss of GroEL function in a temperature-sensitive GroEL mutant strain. Most GroEL interactors are 35-60 kDa in size, consistent with the volume of the GroEL-GroES cavity. Role of chaperonin in evolution, overview |
735322 |
| 5.6.1.7 | malfunction |
cells lacking the zygotic expression of either CCTalpha or CCTdelta show a loss of cell body microtubules, fail to assemble new cilia and die within 2 cell cycles. Loss of CCT subunit activity leads to axoneme shortening and splaying of tips of axonemal microtubules. An epitope-tagged CCTa rescued the gene knockout phenotype and localizes primarily to the tips of cilia |
713358 |
| 5.6.1.7 | malfunction |
enzyme inactivation leads to a drastically reduced accumulation of the ATP synthase complex |
752034 |
| 5.6.1.7 | malfunction |
reduced levels of stromal Hsp70 severely impair plastid development |
749945 |
| 5.6.1.7 | malfunction |
reduced levels of stromal Hsp70 severely impair the plastid development |
749945 |
| 5.6.1.7 | metabolism |
chaperonins are ATP-dependent nanomachines that facilitate protein folding through complex cycles of complex allosteric articulation |
-, 751294 |
| 5.6.1.7 | metabolism |
the enzyme helps protein folding by undergoing a conformational change from a closed state to an open state |
750067 |
