Pseudo-Symmetric Assembly of Protodomains as a Common Denominator in the Evolution of Polytopic Helical Membrane Proteins

Autor:	Philippe Youkharibache, Alexander Tran, Ravinder Abrol
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	0106 biological sciences Pseudo-symmetry FocA Aquaporin Triple helix bundle Computational biology Biology 010603 evolutionary biology 01 natural sciences 7TMH 3TMH SWEET Evolution Molecular 03 medical and health sciences Protein structure GPCR Protein Domains MFS Gene duplication Genetics TRIC Molecular Biology Ecology Evolution Behavior and Systematics 030304 developmental biology G protein-coupled receptor 0303 health sciences Membrane Proteins PnuC Transmembrane protein Divergent evolution Transmembrane domain Membrane protein 7-transmembrane Original Article
Zdroj:	Journal of Molecular Evolution
ISSN:	1432-1432 0022-2844
Popis:	The polytopic helical membrane proteome is dominated by proteins containing seven transmembrane helices (7TMHs). They cannot be grouped under a monolithic fold or superfold. However, a parallel structural analysis of folds around that magic number of seven in distinct protein superfamilies (SWEET, PnuC, TRIC, FocA, Aquaporin, GPCRs) reveals a common homology, not in their structural fold, but in their systematic pseudo-symmetric construction during their evolution. Our analysis leads to guiding principles of intragenic duplication and pseudo-symmetric assembly of ancestral transmembrane helical protodomains, consisting of 3 (or 4) helices. A parallel deconstruction and reconstruction of these domains provides a structural and mechanistic framework for their evolutionary paths. It highlights the conformational plasticity inherent to fold formation itself, the role of structural as well as functional constraints in shaping that fold, and the usefulness of protodomains as a tool to probe convergent vs divergent evolution. In the case of FocA vs. Aquaporin, this protodomain analysis sheds new light on their potential divergent evolution at the protodomain level followed by duplication and parallel evolution of the two folds. GPCR domains, whose function does not seem to require symmetry, nevertheless exhibit structural pseudo-symmetry. Their construction follows the same protodomain assembly as any other pseudo-symmetric protein suggesting their potential evolutionary origins. Interestingly, all the 6/7/8TMH pseudo-symmetric folds in this study also assemble as oligomeric forms in the membrane, emphasizing the role of symmetry in evolution, revealing self-assembly and co-evolution not only at the protodomain level but also at the domain level. Electronic supplementary material The online version of this article (10.1007/s00239-020-09934-4) contains supplementary material, which is available to authorized users.
Databáze:	OpenAIRE
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