ArticleNature structural & molecular biology2017
An information theoretic framework reveals a tunable allosteric network in group II chaperonins.
Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
- Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022Article
- CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.Nature communications · 2021Article
- The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story.Current opinion in structural biology · 2019Review
- Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Identification of an allosteric network that influences assembly and function of group II chaperonins.Nature structural & molecular biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
ATP-dependent allosteric regulation of the ring-shaped group II chaperonins remains ill defined, in part because their complex oligomeric topology has limited the success of structural techniques in suggesting allosteric determinants. Further, their high sequence conservation has hindered the prediction of allosteric networks using mathematical covariation approaches. Here, we develop an information theoretic strategy that is robust to residue conservation and apply it to group II chaperonins. We identify a contiguous network of covarying residues that connects all nucleotide-binding pockets within each chaperonin ring. An interfacial residue between the networks of neighboring subunits controls positive cooperativity by communicating nucleotide occupancy within each ring. Strikingly, chaperonin allostery is tunable through single mutations at this position. Naturally occurring variants at this position that double the extent of positive cooperativity are less prevalent in nature. We propose that being less cooperative than attainable allows chaperonins to support robust folding over a wider range of metabolic conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.