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Role of chaperonin-like proteins in Bardet-Biedl syndrome

Published on October 1, 2007 Reviewed on November 22, 2019   46 min

A selection of talks on Biochemistry

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0:00
Hello, my name is Michel Leroux, I'm an associate professor in the Molecular Biology and Biochemistry Department at Simon Fraser University. Today I'd like to talk to you about the role of chaperonin-like proteins in Bardet-Biedl Syndrome.
0:15
Chaperonins belong to a family of proteins termed 'molecular chaperones', these play various important roles in protein quality control. There are many types of chaperones, here I list three major classes: there is the Hsp70 class, the Hsp60 class (which are also termed chaperonins), as well as Hsp90. Together these play important functions in the cell including folding of proteins, assembly of oligomeric complexes, and targeting of proteins to different subcellular compartments. They also play roles in protein dis-aggregation and protein degradation. In the context of de novo protein folding, Hsp70 and chaperonins play critical roles. As seen in the bottom part of the slide, Hsp70 helps to stabilize polypeptide chains that emerge from the ribosome, whereas chaperonins are thought to mainly assist in post-translational folding of the newly-made polypeptides.
1:17
There are two groups of chaperonins, group I chaperonins are represented by GroEL, which is found in bacteria. Other group I chaperonins include mitochondrial Hsp60 (mtHsp60) and chloroplast Hsp60 (cpHsp60). Group II chaperonins, on the other hand, are present in the eukaryotic and archaeal cytosols. In eukaryotes the main chaperonin is called CCT, or chaperonin containing TCP-1, it is also called TRiC or TCP-1 ring complex. In archaea the cytosolic chaperonin is usually referred to as 'thermosome' because it's particularly abundant under heat shock conditions.
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Role of chaperonin-like proteins in Bardet-Biedl syndrome

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