14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase

T.D. Bunney, H.S. van Walraven, A.H. de Boer

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Mitochondrial and chloroplast ATP synthases are key enzymes in plant metabolism, providing cells with ATP, the universal energy currency. ATP synthases use a transmembrane electrochemical proton gradient to drive synthesis of ATP. The enzyme complexes function as miniature rotary engines, ensuring energy coupling with very high efficiency. Although our understanding of the structure and functioning of the synthase has made enormous progress in recent years, our understanding of regulatory mechanisms is still rather preliminary. Here we report a role for 14-3-3 proteins in the regulation of ATP synthases. These 14-3-3 proteins are highly conserved phosphoserine/phosphothreonine-binding proteins that regulate a wide range of enzymes in plants, animals, and yeast. Recently, the presence of 14-3-3 proteins in chloroplasts was illustrated, and we show here that plant mitochondria harbor 14-3-3s within the inner mitochondrial-membrane compartment. There, the 14-3-3 proteins were found to be associated with the ATP synthases, in a phosphorylation-dependent manner, through direct interaction with the F
Original languageEnglish
Pages (from-to)4249-4254
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
DOIs
Publication statusPublished - 2001

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H-transporting ATP synthase
chloroplasts
proteins
enzymes
energy
engines
protons
binding proteins
phosphorylation
mitochondria
yeasts
metabolism
synthesis
animals
cells

Cite this

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title = "14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase",
abstract = "Mitochondrial and chloroplast ATP synthases are key enzymes in plant metabolism, providing cells with ATP, the universal energy currency. ATP synthases use a transmembrane electrochemical proton gradient to drive synthesis of ATP. The enzyme complexes function as miniature rotary engines, ensuring energy coupling with very high efficiency. Although our understanding of the structure and functioning of the synthase has made enormous progress in recent years, our understanding of regulatory mechanisms is still rather preliminary. Here we report a role for 14-3-3 proteins in the regulation of ATP synthases. These 14-3-3 proteins are highly conserved phosphoserine/phosphothreonine-binding proteins that regulate a wide range of enzymes in plants, animals, and yeast. Recently, the presence of 14-3-3 proteins in chloroplasts was illustrated, and we show here that plant mitochondria harbor 14-3-3s within the inner mitochondrial-membrane compartment. There, the 14-3-3 proteins were found to be associated with the ATP synthases, in a phosphorylation-dependent manner, through direct interaction with the F",
author = "T.D. Bunney and {van Walraven}, H.S. and {de Boer}, A.H.",
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14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase. / Bunney, T.D.; van Walraven, H.S.; de Boer, A.H.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 98, 2001, p. 4249-4254.

Research output: Contribution to JournalArticleAcademicpeer-review

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T1 - 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase

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AU - de Boer, A.H.

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Y1 - 2001

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AB - Mitochondrial and chloroplast ATP synthases are key enzymes in plant metabolism, providing cells with ATP, the universal energy currency. ATP synthases use a transmembrane electrochemical proton gradient to drive synthesis of ATP. The enzyme complexes function as miniature rotary engines, ensuring energy coupling with very high efficiency. Although our understanding of the structure and functioning of the synthase has made enormous progress in recent years, our understanding of regulatory mechanisms is still rather preliminary. Here we report a role for 14-3-3 proteins in the regulation of ATP synthases. These 14-3-3 proteins are highly conserved phosphoserine/phosphothreonine-binding proteins that regulate a wide range of enzymes in plants, animals, and yeast. Recently, the presence of 14-3-3 proteins in chloroplasts was illustrated, and we show here that plant mitochondria harbor 14-3-3s within the inner mitochondrial-membrane compartment. There, the 14-3-3 proteins were found to be associated with the ATP synthases, in a phosphorylation-dependent manner, through direct interaction with the F

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