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A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
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2011 (English)In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 141, no 4, 310-320 p.Article in journal (Refereed) Published
Abstract [en]

The presence of genes encoding organellar proteins in different cellular compartments necessitates a tight coordination of expression by the different genomes of the eukaryotic cell. This coordination of gene expression is achieved by organelle-to-nucleus communication. Stress-induced perturbations of the tetrapyrrole pathway trigger large changes in nuclear gene expression. In order to investigate whether the tetrapyrrole Mg-ProtoIX itself is an important part of plastid-to-nucleus communication, we used an affinity column containing Mg-ProtoIX covalently linked to an Affi-Gel matrix. The proteins that bound to Mg-ProtoIX were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis combined with nano liquid chromatography–mass spectrometry (MS)/MS. Thus, we present a novel proteomic approach to address the mechanisms involved in cellular signaling and we identified interactions between Mg-ProtoIX and a large number of proteins associated with oxidative stress responses. Our approach revealed an interaction between Mg-ProtoIX and the heat shock protein 90-type protein, HSP81-2 suggesting that a regulatory complex including HSP90 proteins and tetrapyrroles controlling gene expression is evolutionarily conserved between yeast and plants. In addition, our list of putative Mg-ProtoIX-binding proteins demonstrated that binding of tetrapyrroles does not depend on a specific amino acid motif but possibly on a specific fold of the protein.

Place, publisher, year, edition, pages
Wiley , 2011. Vol. 141, no 4, 310-320 p.
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Chemical Sciences
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URN: urn:nbn:se:umu:diva-39523DOI: 10.1111/j.1399-3054.2010.01440.xOAI: oai:DiVA.org:umu-39523DiVA: diva2:393453
Note
Article first published online 14 JAN 2011 Available from: 2011-01-31 Created: 2011-01-31 Last updated: 2017-12-11Bibliographically approved

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Kindgren, PeterEriksson, Mats-JerryKieselbach, ThomasStrand, Åsa

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Kindgren, PeterEriksson, Mats-JerryMohapatra, AnasuyaKieselbach, ThomasStrand, Åsa
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Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)Department of Chemistry
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Physiologia Plantarum: An International Journal for Plant Biology
Chemical Sciences

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