AI Article Synopsis
- Chaperonins are large protein complexes with two rings that help other proteins fold correctly.
- There are two types: Type I (found in mitochondria, chloroplasts, and bacteria) and Type II (found in Archaea and eukaryotic cells).
- Protein folding occurs in chaperonins through changes triggered by ATP binding, with CCT focusing on actin and tubulin but also aiding other proteins, possibly collaborating with prefoldin and phosducin-like proteins.
Article Abstract
Chaperonins are large oligomers consisting of two superimposed rings, each enclosing a cavity used for the folding of other proteins. They have been divided into two groups. Chaperonins of type I were identified in mitochondria and chloroplasts (Hsp60) or bacterial cytosol (GroEL) as well. Chaperonins type II were found in Archea and the eukaryotic cell cytosol (CCT). Protein folding occurs in the chaperonin after its conformational changes induced upon ATP binding. Mechanism of the protein folding, although still poorly defined, clearly differs from the one established for GroEL. Although CCT with prefoldin seems to be mainly involved in the folding of actin and tubulin, other substrates engaged in various cellular processes are beginning to be characterized, including proteins possessing WD40-repeats. Moreover, several lines of evidence suggest that beside prefoldin, CCT may work in concert with phosducin-like proteins (PhLPs).
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