Abstract
The recently identified hetero-oligomeric protein complex, named GimC, present in eukarya and archaea, is a critical cofactor of TRiC/CCT-assisted folding of actin and tubulins (1 2). Purification and characterization of this protein complex revealed that its subunits are encoded by six different genes, GIM1 to 6. In vitro studies with purified GimC showed that the protein complex interacts with the eukaryotic chaperonin TRiC/CCT and binds unfolded tubulin and actin, the major substrates of TRiC, but it does not bind to native actin.
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Siegers, K., Schiebel, E. (2000). Purification of GimC from Saccharomyces cerevisiae. In: Schneider, C. (eds) Chaperonin Protocols. Methods in Molecular Biology, vol 140. Humana, Totowa, NJ. https://doi.org/10.1385/1-59259-061-6:185
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DOI: https://doi.org/10.1385/1-59259-061-6:185
Publisher Name: Humana, Totowa, NJ
Print ISBN: 978-0-89603-739-7
Online ISBN: 978-1-59259-061-2
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