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Ribosome Evolution and Structural Capacitance

In addition to the canonical loss-of-function mutations, mutations in proteins may additionally result in gain-of-function through the binary activation of cryptic “structural capacitance elements.” Our previous bioinformatic analysis allowed us to propose a new mechanism of protein evolution – stru...

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Detalles Bibliográficos
Autores principales: Buckle, Ashley M., Buckle, Malcolm
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6872460/
https://www.ncbi.nlm.nih.gov/pubmed/31803754
http://dx.doi.org/10.3389/fmolb.2019.00123
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author Buckle, Ashley M.
Buckle, Malcolm
author_facet Buckle, Ashley M.
Buckle, Malcolm
author_sort Buckle, Ashley M.
collection PubMed
description In addition to the canonical loss-of-function mutations, mutations in proteins may additionally result in gain-of-function through the binary activation of cryptic “structural capacitance elements.” Our previous bioinformatic analysis allowed us to propose a new mechanism of protein evolution – structural capacitance – that arises via the generation of new elements of microstructure upon mutations that cause a disorder-to-order (D→O) transition in previously disordered regions of proteins. Here we propose that the D→O transition is a necessary follow-on from expected early codon-anticodon and tRNA acceptor stem-amino acid usage, via the accumulation of structural capacitance elements – reservoirs of disorder in proteins. We develop this argument further to posit that structural capacitance is an inherent consequence of the evolution of the genetic code.
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spelling pubmed-68724602019-12-04 Ribosome Evolution and Structural Capacitance Buckle, Ashley M. Buckle, Malcolm Front Mol Biosci Molecular Biosciences In addition to the canonical loss-of-function mutations, mutations in proteins may additionally result in gain-of-function through the binary activation of cryptic “structural capacitance elements.” Our previous bioinformatic analysis allowed us to propose a new mechanism of protein evolution – structural capacitance – that arises via the generation of new elements of microstructure upon mutations that cause a disorder-to-order (D→O) transition in previously disordered regions of proteins. Here we propose that the D→O transition is a necessary follow-on from expected early codon-anticodon and tRNA acceptor stem-amino acid usage, via the accumulation of structural capacitance elements – reservoirs of disorder in proteins. We develop this argument further to posit that structural capacitance is an inherent consequence of the evolution of the genetic code. Frontiers Media S.A. 2019-11-14 /pmc/articles/PMC6872460/ /pubmed/31803754 http://dx.doi.org/10.3389/fmolb.2019.00123 Text en Copyright © 2019 Buckle and Buckle. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Buckle, Ashley M.
Buckle, Malcolm
Ribosome Evolution and Structural Capacitance
title Ribosome Evolution and Structural Capacitance
title_full Ribosome Evolution and Structural Capacitance
title_fullStr Ribosome Evolution and Structural Capacitance
title_full_unstemmed Ribosome Evolution and Structural Capacitance
title_short Ribosome Evolution and Structural Capacitance
title_sort ribosome evolution and structural capacitance
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6872460/
https://www.ncbi.nlm.nih.gov/pubmed/31803754
http://dx.doi.org/10.3389/fmolb.2019.00123
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