A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001591
- author
- Kindgren, P. ; Eriksson, M. J. ; Benedict, C. ; Mohapatra, A. ; Gough, S. P. ; Hansson, Mats LU ; Kieselbach, T. and Strand, A.
- publishing date
- 2011
- type
- 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
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:79952374396
- pmid:21158868
- ISSN
- 0031-9317
- DOI
- 10.1111/j.1399-3054.2010.01440.x
- language
- English
- LU publication?
- no
- additional info
- 4
- id
- ccfc6566-6cbe-4087-98af-a3264d8db521 (old id 8001591)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21158868
- date added to LUP
- 2016-04-01 15:01:33
- date last changed
- 2022-01-28 03:43:06
@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}},
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}},
language = {{eng}},
number = {{4}},
pages = {{310--320}},
publisher = {{John Wiley & Sons Inc.}},
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}},
doi = {{10.1111/j.1399-3054.2010.01440.x}},
volume = {{141}},
year = {{2011}},
}