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Chapter 9 The Role of Plastids in Protein Geranylgeranylation in Tobacco BY-2 Cells

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Book cover The Chloroplast

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 31))

Summary

Isoprenylation of proteins, a fundamental process in eukaryotic cells, is characterized by the formation of a thioether bond between the cysteine residue of a carboxyterminal CaaX motif and a C15 (farnesyl) or a C20 (geranylgeranyl) isoprenyl group. Using a rice calmodulin (Oriza sativa CaM61) fragment with a motif for geranylgeranylation, we developed an experimental system allowing us to visualize the localization of isoprenylated proteins in tobacco bright yellow-2 (TBY-2) cells.

Our results clearly demonstrate that the geranylgeranylated proteins are mainly associated with the plasma membrane. Abbrogation of the isoprenylation reaction by inhibitors or mutations in the CaaX box triggers a change in the intracellular targeting of the chimeric proteins, leading to their accumulation in the nucleus instead of at the plasma membrane.

By using specific inhibitors (mevinolin and fosmidomycin) of both isoprenoid precursor pathways occurring in higher plants, we provide evidence for the essential role played by the plastidial methylerythritol phosphate (MEP) pathway in the synthesis of geranylgeranyl diphosphate needed for the covalent modification of such proteins and their association with the plasma membrane in TBY-2 cells. Interestingly, low µM concentrations of exogenous geranylgeraniol were capable of complementing inhibition of the MEP pathway. Such chemical complementation experiments allow for distinguishing between different levels of inhibition, for instance inhibition of precursor biosynthesis versus inhibition of prenyltransferases.

This experimental system can be used to evaluate new herbicides and drugs, which could interact with the MEP pathway or the geranylgeranylation of proteins after having entered the cells and after their potential conversion into an active compound by cellular metabolic processes. It might also be useful in demonstrating toxic effects of specific inhibitors and in measuring biosynthetic fluxes.

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Abbreviations

BD:

basic domain

DMAPP:

dimethylallyl diphosphate

DX:

deoxyxylulose

Fol:

farnesol

FPP:

farnesyl diphosphate

Ftase:

FPP-specific prenyltransferase

GFP:

green fluorescent protein

GFP-BD-CVIL:

GFP, to which the basic domain of rice calmodulin CaM61 bearing a carboxyterminal isoprenylation motif has been fused

GFP-BD-SVIL:

the same, but with the isoprenylation motif disrupted by site-directed mutagenesis

GGol:

geranyl­geraniol

GGPP:

geranylgeranyl diphosphate

GGTase:

I GGPP-specific prenyltransferase type I

IPP:

isopentenyl diphosphate

MEP:

methylerythritol phosphate

MVA:

mevalonic acid

TBY-2:

tobacco Bright Yellow-2

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Acknowledgements

Our work is supported by the CNRS and the Agence Nationale de la Recherche (AH, MR, TJB), by the Université Louis Pasteur (MR) and by the Institut Universitaire de France (MR). We also thank the CNRS, the Université Louis Pasteur, the Région Alsace, and the Association pour la Recherche sur le Cancer for the support of the Inter-Institute confocal microscopy equipment at the IBMP in Strasbourg. We wish to thank Prof. N.-H. Chua for the pTA plasmid, Dr. A.W. Alberts for a generous gift of mevinolin and Dr. R.J. Eilers for a sample of fosmidomycin. We express our thanks to technical staff members at the IBMP’s central services.

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Authors and Affiliations

  1. Département Reseaux Metaboliques, Institut de Botanique, Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (Unité Propre de Recherche 2357 conventionée à l’Université de Strasbourg), 28 rue Goethe, F-67083, Strasbourg, France

    Esther Gerber

  2. Department of Biological Sciences, Idaho State University, 650 Memorial Drive, Pocatello, ID, 83209-8007, USA

    Andréa Hemmerlin

  3. Université de Strasbourg/CNRS, Institut de Chimie (Unité Mixte de Recherche UMR 7177), 4 rue Blaise Pascal, F-67070, Strasbourg, France (MR)

    Thomas J. Bach

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  1. Esther Gerber
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  2. Andréa Hemmerlin
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  3. Thomas J. Bach
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Correspondence to Thomas J. Bach .

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Editors and Affiliations

  1. Rebeiz Foundation for Basic Research, Champaign, USA

    Constantin A. Rebeiz

  2. Michigan State University, East Lansing, USA

    Christoph Benning

  3. University of Illinois at Urbana-Champaign, Urbana, USA

    Hans J. Bohnert

  4. Central Florida University, Orlando, USA

    Henry Daniell

  5. Arizona State University, Tempe, USA

    J. Kenneth Hoober

  6. University of Karlsruhe, Germany

    Hartmut K. Lichtenthaler

  7. University of Illinois at Urbana-Champaign, Urbana, USA

    Archie R. Portis

  8. Jawaharlal Nehru University, New Delhi, India

    Baishnab C. Tripathy

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Gerber, E., Hemmerlin, A., Bach, T.J. (2010). Chapter 9 The Role of Plastids in Protein Geranylgeranylation in Tobacco BY-2 Cells. In: Rebeiz, C.A., et al. The Chloroplast. Advances in Photosynthesis and Respiration, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-8531-3_9

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