Symmetry‐free cryo‐EM structures of the chaperonin TRiC along its ATPase‐driven conformational cycle
The eukaryotic group II chaperonin TRiC/CCT is a 16‐subunit complex with eight distinct but
similar subunits arranged in two stacked rings. Substrate folding inside the central chamber …
similar subunits arranged in two stacked rings. Substrate folding inside the central chamber …
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM
The eukaryotic chaperonin TRiC (or CCT) assists in the folding of 10% of cytosolic proteins.
Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly …
Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly …
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
All chaperonins mediate ATP-dependent polypeptide folding by confining substrates within
a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a …
a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a …
[HTML][HTML] A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle
S Reissmann, LA Joachimiak, B Chen, AS Meyer… - Cell reports, 2012 - cell.com
The eukaryotic chaperonin TRiC/CCT uses ATP cycling to fold many essential proteins that
other chaperones cannot fold. This 1 MDa hetero-oligomer consists of two identical stacked …
other chaperones cannot fold. This 1 MDa hetero-oligomer consists of two identical stacked …
4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement
Y Cong, ML Baker, J Jakana… - Proceedings of the …, 2010 - National Acad Sciences
The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or
chaperonin containing TCP1) assists the folding of∼ 5–10% of the cellular proteome. Many …
chaperonin containing TCP1) assists the folding of∼ 5–10% of the cellular proteome. Many …
Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling
N Kalisman, CM Adams… - Proceedings of the …, 2012 - National Acad Sciences
The TRiC/CCT chaperonin is a 1-MDa hetero-oligomer of 16 subunits that assists the folding
of proteins in eukaryotes. Low-resolution structural studies confirmed the TRiC particle to be …
of proteins in eukaryotes. Low-resolution structural studies confirmed the TRiC particle to be …
[HTML][HTML] State-dependent sequential allostery exhibited by chaperonin TRiC/CCT revealed by network analysis of Cryo-EM maps
The eukaryotic chaperonin TRiC/CCT plays a major role in assisting the folding of many
proteins through an ATP-driven allosteric cycle. Recent structures elucidated by cryo …
proteins through an ATP-driven allosteric cycle. Recent structures elucidated by cryo …
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
A Leitner, LA Joachimiak, A Bracher, L Mönkemeyer… - Structure, 2012 - cell.com
TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate
folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric …
folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric …
Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns
MP Collier, KB Moreira, KH Li, YC Chen, D Itzhak… - Scientific Reports, 2021 - nature.com
The eukaryotic chaperonin TRiC/CCT is a large ATP-dependent complex essential for
cellular protein folding. Its subunit arrangement into two stacked eight-membered hetero …
cellular protein folding. Its subunit arrangement into two stacked eight-membered hetero …
The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story
Highlights•The eukaryotic chaperonin TRiC/CCT is a large hetero-oligomeric ring-shaped
complex.•TRiC uses ATP to fold many essential cellular proteins within its central …
complex.•TRiC uses ATP to fold many essential cellular proteins within its central …