A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress

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A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress. / Kindgren, P.; Eriksson, M. J.; Benedict, C.; Mohapatra, A.; Gough, S. P.; Hansson, Mats; Kieselbach, T.; Strand, A.

I: Physiologia Plantarum, Vol. 141, Nr. 4, 2011, s. 310-320.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Harvard

Kindgren, P, Eriksson, MJ, Benedict, C, Mohapatra, A, Gough, SP, Hansson, M, Kieselbach, T & Strand, A 2011, 'A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress', Physiologia Plantarum, vol. 141, nr. 4, s. 310-320. https://doi.org/10.1111/j.1399-3054.2010.01440.x

APA

Kindgren, P., Eriksson, M. J., Benedict, C., Mohapatra, A., Gough, S. P., Hansson, M., Kieselbach, T., & Strand, A. (2011). A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress. Physiologia Plantarum, 141(4), 310-320. https://doi.org/10.1111/j.1399-3054.2010.01440.x

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MLA

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Author

Kindgren, P. ; Eriksson, M. J. ; Benedict, C. ; Mohapatra, A. ; Gough, S. P. ; Hansson, Mats ; Kieselbach, T. ; Strand, A. / A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress. I: Physiologia Plantarum. 2011 ; Vol. 141, Nr. 4. s. 310-320.

RIS

TY - JOUR

T1 - A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress

AU - Kindgren, P.

AU - Eriksson, M. J.

AU - Benedict, C.

AU - Mohapatra, A.

AU - Gough, S. P.

AU - Hansson, Mats

AU - Kieselbach, T.

AU - Strand, A.

N1 - 4

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

KW - Protoporphyrins/metabolism

KW - Proteomics/methods

KW - Protein Subunits/metabolism

KW - Protein Binding

KW - Oxidative Stress

KW - Lyases/metabolism

KW - Light-Harvesting Protein Complexes/metabolism

KW - Plant

KW - Gene Expression Regulation

KW - Computational Biology

KW - Western

KW - Blotting

KW - Arabidopsis Proteins/genetics/metabolism

KW - Amino Acid Motifs

KW - Arabidopsis/enzymology/genetics

KW - Reproducibility of Results

KW - Signal Transduction

KW - Spectrometry

KW - Fluorescence

KW - Stress

KW - Physiological

KW - Tetrapyrroles/metabolism

U2 - 10.1111/j.1399-3054.2010.01440.x

DO - 10.1111/j.1399-3054.2010.01440.x

M3 - Article

C2 - 21158868

VL - 141

SP - 310

EP - 320

JO - Physiologia Plantarum

JF - Physiologia Plantarum

SN - 0031-9317

IS - 4

ER -