ATP synthase: evolution, energetics, and membrane interactions

TL;DR

This review discusses the evolution, structure, and function of F-type ATP synthases, emphasizing their adaptations across different organisms and the importance of membrane environment interactions for understanding these essential enzymes.

Contribution

It provides an integrated overview of ATP synthase structure, function, evolution, and membrane interactions, highlighting adaptations across taxa and the significance of lipid environments.

Findings

ATP synthases are highly conserved across all domains of life.

Membrane environment significantly influences ATP synthase structure and function.

Adaptations of ATP synthases are linked to diverse habitats and evolutionary pressures.

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 is believed to predate the divergence of these lineages over 1.5 billion years ago. These enzymes have therefore facilitated the survival of organisms in a wide range of habitats, ranging from the deep-sea thermal vents to the human intestine. In this review, we present an overview of the current knowledge of the structure and function of F-type ATPases, highlighting several adaptations that have been characterized across taxa. 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.