-
Tytuł:
-
Structural and functional properties of plant mitochondrial F-ATP synthase.
-
Autorzy:
-
Zancani M; Department of Agriculture, Food, Environmental and Animal Sciences, Plant Biology Unit, University of Udine, via delle Scienze 91, 33100 Udine, Italy. Electronic address: .
Braidot E; Department of Agriculture, Food, Environmental and Animal Sciences, Plant Biology Unit, University of Udine, via delle Scienze 91, 33100 Udine, Italy.
Filippi A; Department of Agriculture, Food, Environmental and Animal Sciences, Plant Biology Unit, University of Udine, via delle Scienze 91, 33100 Udine, Italy.
Lippe G; Department of Agriculture, Food, Environmental and Animal Sciences, Plant Biology Unit, University of Udine, via delle Scienze 91, 33100 Udine, Italy.
-
Źródło:
-
Mitochondrion [Mitochondrion] 2020 Jul; Vol. 53, pp. 178-193. Date of Electronic Publication: 2020 Jun 11.
-
Typ publikacji:
-
Journal Article; Research Support, Non-U.S. Gov't; Review
-
Język:
-
English
-
Imprint Name(s):
-
Original Publication: Amsterdam ; New York : Elsevier Science, c2001-
-
MeSH Terms:
-
Plants/*enzymology
Proton-Translocating ATPases/*chemistry
Proton-Translocating ATPases/*metabolism
Gene Expression Regulation, Enzymologic ; Mitochondria/metabolism ; Models, Molecular ; Plant Proteins/chemistry ; Plant Proteins/metabolism ; Plants/chemistry ; Protein Conformation ; Stress, Physiological
-
Contributed Indexing:
-
Keywords: ATP; Complex V; Dimer; F-ATP synthase; PTP; Plant mitochondria; Stress
-
Substance Nomenclature:
-
0 (Plant Proteins)
EC 3.6.3.14 (Proton-Translocating ATPases)
-
Entry Date(s):
-
Date Created: 20200614 Date Completed: 20210329 Latest Revision: 20210329
-
Update Code:
-
20240105
-
DOI:
-
10.1016/j.mito.2020.06.001
-
PMID:
-
32534049
-
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 (F 1 ), located in the mitochondrial matrix, a membrane-bound part (F O ), 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.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.)
