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Mutation in the cysteine bridge domain of the γ-subunit affects light regulation of the ATP synthase but not photosynthesis or growth in Arabidopsis

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Abstract

The chloroplast ATP synthase synthesizes ATP from ADP and free phosphate coupled by the electrochemical potential across the thylakoid membrane in the light. The light-dependent regulation of ATP synthase activity is carried out in part through redox modulation of a cysteine disulfide bridge in CF1 γ-subunit. In order to investigate the function of the redox regulatory domain and the physiological significance of redox modulation for higher plants, we designed four mutations in the redox regulatory domain of the γ-subunit to create functional mimics of the permanently reduced form of the γ-subunit. While the inability to reduce the regulatory disulfide results in lower photosynthesis and growth, unexpectedly, the results reported here show that inability to reoxidize the dithiol may not be of any direct detriment to plant photosynthetic performance or growth.

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Abbreviations

CF1 :

Coupling factor 1

DCCD:

N, N′-Dicyclohexylcarbodiimide

DTT:

Dithiothreitol

RT-PCR:

Reverse transcript polymerase chain reaction

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Acknowledgments

We thank Dr. Aleel Grennan for her expert assistance with the manuscript.

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Author notes

  1. Guosheng Wu

    Present address: Department of Botany, University of Wisconsin, Madison, WI, 53706, USA

Authors and Affiliations

  1. Department of Plant Biology, University of Illinois, 1201 W. Gregory Dr., Urbana, IL, 61801, USA

    Guosheng Wu & Donald R. Ort

  2. Photosynthesis Research Unit, USDA Agricultural Research Service, Urbana, IL, 61801, USA

    Donald R. Ort

Authors
  1. Guosheng Wu
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  2. Donald R. Ort
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Correspondence to Donald R. Ort.

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Wu, G., Ort, D.R. Mutation in the cysteine bridge domain of the γ-subunit affects light regulation of the ATP synthase but not photosynthesis or growth in Arabidopsis. Photosynth Res 97, 185–193 (2008). https://doi.org/10.1007/s11120-008-9315-0

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  • DOI: https://doi.org/10.1007/s11120-008-9315-0

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