Structural and functional properties of plant mitochondrial F-ATP synthase

Mitochondrion. 2020 Jul:53:178-193. doi: 10.1016/j.mito.2020.06.001. Epub 2020 Jun 11.

Abstract

The mitochondrial F-ATP synthase is responsible for coupling the transmembrane proton gradient, generated through the inner membrane by the electron transport chain, to the synthesis of ATP. This enzyme shares a basic architecture with the prokaryotic and chloroplast ones, since it is composed of a catalytic head (F1), located in the mitochondrial matrix, a membrane-bound part (FO), together with a central and a peripheral stalk. In this review we compare the structural and functional properties of F-ATP synthase in plant mitochondria with those of yeast and mammals. We also present the physiological impact of the alteration of F-ATP synthase in plants, with a special regard to its involvement in cytoplasmic male sterility. Furthermore, we show the involvement of this enzyme in plant stress responses. Finally, we discuss the role of F-ATP synthase in shaping the curvature of the mitochondrial inner membrane and in permeability transition pore formation.

Keywords: ATP; Complex V; Dimer; F-ATP synthase; PTP; Plant mitochondria; Stress.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Gene Expression Regulation, Enzymologic
  • Mitochondria / metabolism
  • Models, Molecular
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Plants / chemistry
  • Plants / enzymology*
  • Protein Conformation
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / metabolism*
  • Stress, Physiological

Substances

  • Plant Proteins
  • Proton-Translocating ATPases