ArticleScientific reports2018
Development of a yeast internal-subunit eGFP labeling strategy and its application in subunit identification in eukaryotic group II chaperonin TRiC/CCT.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- Article
- The conformational landscape of TRiC ring-opening and its underlying stepwise mechanism revealed by cryo-EM.QRB discovery · 2025Article
- Lassa virus Z protein hijacks the autophagy machinery for efficient transportation by interrupting CCT2-mediated cytoskeleton network formation.Autophagy · 2024Article
- The CCT chaperonin and actin modulate the ER and RNA-binding protein condensation during oogenesis and maintain translational repression of maternal mRNA and oocyte quality.Molecular biology of the cell · 2024Article
- Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.Communications biology · 2023Article
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
- Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- State-dependent sequential allostery exhibited by chaperonin TRiC/CCT revealed by network analysis of Cryo-EM maps.Progress in biophysics and molecular biology · 2021Article
- Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ.Nature communications · 2021Article
- Interpretation of medium resolution cryoEM maps of multi-protein complexes.Current opinion in structural biology · 2019Review
- An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Advances in domain and subunit localization technology for electron microscopy.Biophysical reviews · 2019Review
- Architecture and subunit arrangement of the complete Saccharomyces cerevisiae COMPASS complex.Scientific reports · 2018Article
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8 authors.
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Abstract
Unambiguous subunit assignment in a multicomponent complex is critical for thorough understanding of the machinery and its functionality. The eukaryotic group II chaperonin TRiC/CCT folds approximately 10% of cytosolic proteins and is important for the maintenance of cellular homeostasis. TRiC consists of two rings and each ring has eight homologous but distinct subunits. Unambiguous subunit identification of a macromolecular machine such as TRiC through intermediate or low-resolution cryo-EM map remains challenging. Here we present a yeast internal-subunit eGFP labeling strategy termed YISEL, which can quickly introduce an eGFP tag in the internal position of a target subunit by homologous recombination, and the tag labeled protein can be expressed in endogenous level. Through this method, the labeling efficiency and tag-occupancy is ensured, and the inserted tag is usually less mobile compared to that fused to the terminus. It can also be used to bio-engineer other tag in the internal position of a protein in yeast. By applying our YISEL strategy and combined with cryo-EM 3D reconstruction, we unambiguously identified all the subunits in the cryo-EM map of TRiC, demonstrating the potential for broad application of this strategy in accurate and efficient subunit identification in other challenging complexes.
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