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Quantitative analysis of protein turnover in plants

Authors

  • Clark J. Nelson,

    1. ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, WA, Australia
    2. Centre for Comparative Analysis of Biomolecular Networks, University of Western Australia, WA, Australia
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  • Lei Li,

    1. ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, WA, Australia
    2. Centre for Comparative Analysis of Biomolecular Networks, University of Western Australia, WA, Australia
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  • A. Harvey Millar

    Corresponding author
    1. ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, WA, Australia
    2. Centre for Comparative Analysis of Biomolecular Networks, University of Western Australia, WA, Australia
    • Correspondence: Dr. A. Harvey Millar, The University of Western Australia, M316, 35 Stirling Highway, Crawley WA 6009, Western Australia, Australia

      E-mail: harvey.millar@uwa.edu.au

      Fax: +61 8 64884401

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Abstract

Proteins are constantly being synthesised and degraded as plant cells age and as plants grow, develop and adapt the proteome. Given that plants develop through a series of events from germination to fruiting and even undertake whole organ senescence, an understanding of protein turnover as a fundamental part of this process in plants is essential. Both synthesis and degradation processes are spatially separated in a cell across its compartmented structure. The majority of protein synthesis occurs in the cytosol, while synthesis of specific components occurs inside plastids and mitochondria. Degradation of proteins occurs in both the cytosol, through the action of the plant proteasome, and in organelles and lytic structures through different protease classes. Tracking the specific synthesis and degradation rate of individual proteins can be undertaken using stable isotope feeding and the ability of peptide MS to track labelled peptide fractions over time. Mathematical modelling can be used to follow the isotope signature of newly synthesised protein as it accumulates and natural abundance proteins as they are lost through degradation. Different technical and biological constraints govern the potential for the use of 13C, 15N, 2H and 18O for these experiments in complete labelling and partial labelling strategies. Future development of quantitative protein turnover analysis will involve analysis of protein populations in complexes and subcellular compartments, assessing the effect of PTMs and integrating turnover studies into wider system biology study of plants.

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