ATP synthase: Evolution, energetics, and membrane interactions

Author:

Nirody Jasmine A.12ORCID,Budin Itay3ORCID,Rangamani Padmini4ORCID

Affiliation:

1. Center for Studies in Physics and Biology, The Rockefeller University, New York, NY

2. All Souls College, University of Oxford, Oxford, UK

3. Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA

4. Department of Mechanical and Aerospace Engineering, University of California San Diego, La Jolla, CA

Abstract

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.

Funder

James S. McDonnell Foundation

The Rockefeller University

All Souls College

National Science Foundation

Air Force Office of Scientific Research

Publisher

Rockefeller University Press

Subject

Physiology

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