Supplemental Information for Lopez, Dalton et al. "An information theoretic framework reveals a tunable allosteric network in the group II chaperonins"

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Abstract/Contents

Abstract
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.

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Type of resource software, multimedia
Date created May 16, 2017

Creators/Contributors

Author Dalton, Kevin
Author Lopez, Tom
Author Tomlinson, Anthony
Principal investigator Frydman, Judith
Principal investigator Pande, Vijay

Subjects

Subject evolution
Subject protein
Subject allostery
Subject chaperonin
Subject information theory
Subject Department of Biology
Subject Department of Chemistry
Genre Dataset

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This work is licensed under a Creative Commons Attribution 3.0 Unported license (CC BY).

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