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  A metabolic probe-enabled strategy reveals uptake and protein targets of polyunsaturated aldehydes in the diatom Phaeodactylum tricornutum

Wolfram, S., Wielsch, N., Hupfer, Y., Mönch, B., Lu-Walther, H.-W., Heintzmann, R., et al. (2015). A metabolic probe-enabled strategy reveals uptake and protein targets of polyunsaturated aldehydes in the diatom Phaeodactylum tricornutum. PLoS One, 10(10): e0140927. doi:10.1371/journal.pone.0140927.

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http://dx.doi.org/10.1371/journal.pone.0140927 (Publisher version)
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Wolfram, Stefanie, Author
Wielsch, Natalie1, Author              
Hupfer, Yvonne1, Author              
Mönch, Bettina, Author
Lu-Walther, Hui-Wen, Author
Heintzmann, Rainer, Author
Werz, Oliver, Author
Svatoš, Aleš1, Author              
Pohnert, Georg2, Author              
Affiliations:
1Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society, ou_421899              
2External Organizations, ou_persistent22              

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 Abstract: Diatoms are unicellular algae of crucial importance as they belong to the main primary producers in aquatic ecosystems. Several diatom species produce polyunsaturated aldehydes (PUAs) that have been made responsible for chemically mediated interactions in the plankton. PUA-effects include chemical defense by reducing the reproductive success of grazing copepods, allelochemical activity by interfering with the growth of competing phytoplankton and cell to cell signaling. We applied a PUA-derived molecular probe, based on the biologically highly active 2,4-decadienal, with the aim to reveal protein targets of PUAs and affected metabolic pathways. By using fluorescence microscopy, we observed a substantial uptake of the PUA probe into cells of the diatom Phaeodactylum tricornutum in comparison to the uptake of a structurally closely related control probe based on a saturated aldehyde. The specific uptake motivated a chemoproteomic approach to generate a qualitative inventory of proteins covalently targeted by the α,β,γ,δ-unsaturated aldehyde structure element. Activity-based protein profiling revealed selective covalent modification of target proteins by the PUA probe. Analysis of the labeled proteins gave insights into putative affected molecular functions and biological processes such as photosynthesis including ATP generation and catalytic activity in the Calvin cycle or the pentose phosphate pathway. The mechanism of action of PUAs involves covalent reactions with proteins that may result in protein dysfunction and interference of involved pathways.

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 Dates: 2015-10-012015-10-232015-11
 Publication Status: Published in print
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 Identifiers: Other: MS175
DOI: 10.1371/journal.pone.0140927
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Title: PLoS One
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 10 (10) Sequence Number: e0140927 Start / End Page: - Identifier: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850