Supplemental Information for Lopez, Dalton et al. "An information theoretic framework reveals a tunable allosteric network in the group II chaperonins"
- Group II chaperonins are ring-shaped chaperones. Their ATP-dependent allosteric regulation remains ill-defined. Given their complex oligomeric topology, structural techniques have had limited success in suggesting allosteric determinants. High sequence conservation among chaperonins has also hindered the prediction of allosteric networks, as many mathematical covariation approaches cannot be applied to conserved proteins. Here, we develop an information theoretic strategy 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. Strikingly, chaperonin allostery is tunable through mutations at this position. Naturally occurring variants that double the extent of positive cooperativity are less prevalent in nature. We propose that being less cooperative that attainable allows the chaperonins to support robust folding over a wider range of metabolic conditions.
|Type of resource
|May 16, 2017
|Department of Biology
|Department of Chemistry
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