AUTHOR=Taguchi Hideki , Koike-Takeshita Ayumi TITLE=In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution JOURNAL=Frontiers in Molecular Biosciences VOLUME=10 YEAR=2023 URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2023.1091677 DOI=10.3389/fmolb.2023.1091677 ISSN=2296-889X ABSTRACT=
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating central cavities to accommodate client proteins (also referred as substrate proteins) for folding. GroEL and GroES (GroE) are the only indispensable chaperones for bacterial viability, except for some species of Mollicutes such as