InterPro domain: IPR009053

The Prefoldin/GimC family of proteins are found in eukaryotes and archaea [ 1 ]. Prefoldin is part of a molecular chaperone system that promotes the correct folding of nascent polypeptide chains. Prefoldin/GimC interacts with the nascent chain to stabilise it prior to its folding within the central cavity of a chaperonin. Prefoldin/GimC is a hexamer consisting of two types of subunits, alpha and beta. Archaeal prefoldin contains one type of alpha and one type of beta subunit [ 2 ], while eukaryotic prefoldin/GimC contains two different but related alpha subunits and four related beta subunits [ 3 ].

The unconventional prefoldin RPB5 interactor-like protein from Drosophila (also known as URI) is a serine/threonine phosphatase inhibitor and required for germ line cell viability and differentiation. It binds to protein phosphatase 1 alpha subunits with higher affinity than the beta subunits [ 4 ].

1. A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J. 17, 952-66
2. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-32
3. Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. EMBO J. 21, 6377-86
4. Drosophila Uri, a PP1alpha binding protein, is essential for viability, maintenance of DNA integrity and normal transcriptional activity. BMC Mol. Biol. 9, 36