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  A genetically validated approach to detect inorganic polyphosphates in plants

Zhu, J., Loubéry, S., Broger, L., Zhang, Y., Lorenzo-Orts, L., Utz-Pugin, A., et al. (2020). A genetically validated approach to detect inorganic polyphosphates in plants. The Plant Journal, 102(3), 507-516. doi:10.1111/tpj.14642.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-6C50-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-5CF3-1
Genre: Journal Article

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 Creators:
Zhu, Jinsheng1, Author
Loubéry, Sylvain1, Author
Broger, Larissa1, Author
Zhang, YJ2, Author              
Lorenzo-Orts, Laura1, Author
Utz-Pugin, Anne1, Author
Fernie, A. R.2, Author              
Young-Tae, Chang1, Author
Hothorn, Michael1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              

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Free keywords: inorganic polyphosphate, energy metabolism, polyphosphate kinase, polyphosphate phosphatase, Arabidopsis, Chlamydomonas
 Abstract: Abstract Inorganic polyphosphates (polyPs) are linear polymers of orthophosphate units linked by phosphoanhydride bonds. PolyPs represent important stores of phosphate and energy, and are abundantly found in many pro- and eukaryotic organisms. In plants, the existence of polyPs has been established using microscopy and biochemical extraction methods that are now known to produce artifacts. Here we use a polyP-specific dye and a polyP binding domain to detect polyPs in plant and algal cells. To develop the staining protocol, we induced polyP granules in Nicotiana benthamiana and Arabiopsis cells by heterologous expression of E. coli polyphosphate kinase 1 (PPK1). Over-expression of PPK1 but not of a catalytically impaired version of the enzyme lead to severe growth phenotypes, suggesting that ATP-dependent synthesis and accumulation of polyPs in the plant cytosol is toxic. We next crossed stable PPK1 expressing Arabidopsis lines with plants expressing the polyP-binding domain of E. coli exopolyphosphatase (PPX1c), which co-localized with PPK1-generated polyP granules. These granules were stained by the polyP-specific dye JC-D7 and appeared as electron dense structures in transmission electron microscopy (TEM) sections. Using the polyP staining protocol derived from these experiments, we screened for polyP stores in different organs and tissues of both mono- and dicotyledonous plants. While we could not detect polyP granules in higher plants, we could visualize the polyP-rich acidocalicisomes in the green algae Chlamydomonas reinhardtii.

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Language(s): eng - English
 Dates: 20192020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1111/tpj.14642
BibTex Citekey: doi:10.1111/tpj.14642
 Degree: -

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Title: The Plant Journal
  Other : Plant J.
Source Genre: Journal
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Publ. Info: Oxford : Blackwell Science
Pages: - Volume / Issue: 102 (3) Sequence Number: - Start / End Page: 507 - 516 Identifier: ISSN: 0960-7412
CoNE: https://pure.mpg.de/cone/journals/resource/954925579095_1