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ATP synthase: Evolution, energetics, and membrane interactions
The synthesis of ATP, life’s “universal energy currency,” is the most prevalent chemical reaction in biological systems and is responsible for fueling nearly all cellular processes, from nerve impulse propagation to DNA synthesis. ATP synthases, the family of enzymes that carry out this endless task...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7594442/ https://www.ncbi.nlm.nih.gov/pubmed/32966553 http://dx.doi.org/10.1085/jgp.201912475 |
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author | Nirody, Jasmine A. Budin, Itay Rangamani, Padmini |
author_facet | Nirody, Jasmine A. Budin, Itay Rangamani, Padmini |
author_sort | Nirody, Jasmine A. |
collection | PubMed |
description | The synthesis of ATP, life’s “universal energy currency,” is the most prevalent chemical reaction in biological systems and is responsible for fueling nearly all cellular processes, from nerve impulse propagation to DNA synthesis. ATP synthases, the family of enzymes that carry out this endless task, are nearly as ubiquitous as the energy-laden molecule they are responsible for making. The F-type ATP synthase (F-ATPase) is found in every domain of life and has facilitated the survival of organisms in a wide range of habitats, ranging from the deep-sea thermal vents to the human intestine. Accordingly, there has been a large amount of work dedicated toward understanding the structural and functional details of ATP synthases in a wide range of species. Less attention, however, has been paid toward integrating these advances in ATP synthase molecular biology within the context of its evolutionary history. In this review, we present an overview of several structural and functional features of the F-type ATPases that vary across taxa and are purported to be adaptive or otherwise evolutionarily significant: ion channel selectivity, rotor ring size and stoichiometry, ATPase dimeric structure and localization in the mitochondrial inner membrane, and interactions with membrane lipids. We emphasize the importance of studying these features within the context of the enzyme’s particular lipid environment. Just as the interactions between an organism and its physical environment shape its evolutionary trajectory, ATPases are impacted by the membranes within which they reside. We argue that a comprehensive understanding of the structure, function, and evolution of membrane proteins—including ATP synthase—requires such an integrative approach. |
format | Online Article Text |
id | pubmed-7594442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-75944422021-05-02 ATP synthase: Evolution, energetics, and membrane interactions Nirody, Jasmine A. Budin, Itay Rangamani, Padmini J Gen Physiol Review The synthesis of ATP, life’s “universal energy currency,” is the most prevalent chemical reaction in biological systems and is responsible for fueling nearly all cellular processes, from nerve impulse propagation to DNA synthesis. ATP synthases, the family of enzymes that carry out this endless task, are nearly as ubiquitous as the energy-laden molecule they are responsible for making. The F-type ATP synthase (F-ATPase) is found in every domain of life and has facilitated the survival of organisms in a wide range of habitats, ranging from the deep-sea thermal vents to the human intestine. Accordingly, there has been a large amount of work dedicated toward understanding the structural and functional details of ATP synthases in a wide range of species. Less attention, however, has been paid toward integrating these advances in ATP synthase molecular biology within the context of its evolutionary history. In this review, we present an overview of several structural and functional features of the F-type ATPases that vary across taxa and are purported to be adaptive or otherwise evolutionarily significant: ion channel selectivity, rotor ring size and stoichiometry, ATPase dimeric structure and localization in the mitochondrial inner membrane, and interactions with membrane lipids. We emphasize the importance of studying these features within the context of the enzyme’s particular lipid environment. Just as the interactions between an organism and its physical environment shape its evolutionary trajectory, ATPases are impacted by the membranes within which they reside. We argue that a comprehensive understanding of the structure, function, and evolution of membrane proteins—including ATP synthase—requires such an integrative approach. Rockefeller University Press 2020-09-23 /pmc/articles/PMC7594442/ /pubmed/32966553 http://dx.doi.org/10.1085/jgp.201912475 Text en © 2020 Nirody et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Review Nirody, Jasmine A. Budin, Itay Rangamani, Padmini ATP synthase: Evolution, energetics, and membrane interactions |
title | ATP synthase: Evolution, energetics, and membrane interactions |
title_full | ATP synthase: Evolution, energetics, and membrane interactions |
title_fullStr | ATP synthase: Evolution, energetics, and membrane interactions |
title_full_unstemmed | ATP synthase: Evolution, energetics, and membrane interactions |
title_short | ATP synthase: Evolution, energetics, and membrane interactions |
title_sort | atp synthase: evolution, energetics, and membrane interactions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7594442/ https://www.ncbi.nlm.nih.gov/pubmed/32966553 http://dx.doi.org/10.1085/jgp.201912475 |
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