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4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement
4.0-A resolution cryo-EM structure mammalian chaperonin TRiC/CCT reveals unique subunit arrangement
2015/12/11
The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or chaperonin containing TCP1) assists the folding of approximately 5-10% of the cellular proteome. Many TRiC substrates can...
A Direct Regulatory Interaction between Chaperonin TRiC and Stress-Responsive Transcription Factor HSF1
Direct Regulatory Interaction TRiC Stress-Responsive Transcription Factor HSF1
2015/12/11
Heat shock transcription factor 1 (HSF1) is an evolutionarily conserved transcription factor that protects cells from protein-misfolding-induced stress and apoptosis. The mechanisms by which cytosolic...