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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 LU ; Kieselbach, T. and Strand, A. (2011) In Physiologia Plantarum 141(4). p.310-320
Abstract
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... (More)
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. (Less)
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author
publishing date
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Contribution to journal
publication status
published
subject
keywords
Protoporphyrins/*metabolism, Proteomics/*methods, Protein Subunits/metabolism, Protein Binding, *Oxidative Stress, Lyases/metabolism, Light-Harvesting Protein Complexes/metabolism, Plant, Gene Expression Regulation, Computational Biology, Western, Blotting, Arabidopsis Proteins/genetics/metabolism, Amino Acid Motifs, Arabidopsis/enzymology/genetics, Reproducibility of Results, Signal Transduction, Spectrometry, Fluorescence, Stress, Physiological, Tetrapyrroles/metabolism
in
Physiologia Plantarum
volume
141
issue
4
pages
310 - 320
publisher
Wiley Online Library
external identifiers
  • scopus:79952374396
ISSN
0031-9317
DOI
10.1111/j.1399-3054.2010.01440.x
language
English
LU publication?
no
id
ccfc6566-6cbe-4087-98af-a3264d8db521 (old id 8001591)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21158868
date added to LUP
2015-09-30 15:09:12
date last changed
2017-03-05 04:00:45
@article{ccfc6566-6cbe-4087-98af-a3264d8db521,
  abstract     = {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.},
  author       = {Kindgren, P. and Eriksson, M. J. and Benedict, C. and Mohapatra, A. and Gough, S. P. and Hansson, Mats and Kieselbach, T. and Strand, A.},
  issn         = {0031-9317},
  keyword      = {Protoporphyrins/*metabolism,Proteomics/*methods,Protein Subunits/metabolism,Protein Binding,*Oxidative Stress,Lyases/metabolism,Light-Harvesting Protein Complexes/metabolism,Plant,Gene Expression Regulation,Computational Biology,Western,Blotting,Arabidopsis Proteins/genetics/metabolism,Amino Acid Motifs,Arabidopsis/enzymology/genetics,Reproducibility of Results,Signal Transduction,Spectrometry,Fluorescence,Stress,Physiological,Tetrapyrroles/metabolism},
  language     = {eng},
  number       = {4},
  pages        = {310--320},
  publisher    = {Wiley Online Library},
  series       = {Physiologia Plantarum},
  title        = {A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress},
  url          = {http://dx.doi.org/10.1111/j.1399-3054.2010.01440.x},
  volume       = {141},
  year         = {2011},
}