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Transmembrane helix helix interactions mediate the folding and assembly of membrane proteins.
Slm9 affinity purifications also revealed interactions with subunits of the chaperonin CCT, which is known to mediate the folding of numerous proteins [23].
HSP70 and its family members mediate the folding of newly translated proteins in the cytosol and organelles [57], [58] and also have been reported to promote ARE-mediated mRNA decay [59], [60].
Also CCT may mediate the folding of 1000 2000 other proteins that play diverse and critical functions in the cell, as, for example, cell cycle progression, chromatin remodeling, assembly of nuclear pore complex and protein degradation [35], [36].
Since chaperonins are known to mediate the folding of cytoskeletal actin, as an initial study we determined the mRNA and protein levels of α-SMA in fetal and adult fibroblasts.
AHA1 is not the only protein that interacts with chaperones to mediate the folding of CFTR.
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We propose that TRiC mediates the folding of cytosolic proteins by a mechanism distinct from that of the chaperonins in specific aspects.
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol.
The GroEL protein mediates the folding of polypeptides, and it is found to be highly expressed in Buchnera and other p-endosymbionts.
Together with vitronectin, clusterin is a component of the terminal complement complex and mediates the folding of extracellular proteins as a chaperone [26].
A network of highly conserved molecules, termed chaperones and co-chaperones, mediates the folding and re-folding of proteins and thus is critical for preserving the functional state and structure of client proteins [ 52– 52].
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