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

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

Paper doi abstract bibtex

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.

@article{kindgren_novel_2011,
	title = {A novel proteomic approach reveals a role for {Mg}-protoporphyrin {IX} in response to oxidative stress},
	volume = {141},
	issn = {1399-3054},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1399-3054.2010.01440.x},
	doi = {10/d2cw82},
	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.},
	language = {en},
	number = {4},
	urldate = {2021-09-02},
	journal = {Physiologia Plantarum},
	author = {Kindgren, Peter and Eriksson, Mats-Jerry and Benedict, Catherine and Mohapatra, Anasuya and Gough, Simon P. and Hansson, Mats and Kieselbach, Thomas and Strand, Åsa},
	year = {2011},
	note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3054.2010.01440.x},
	pages = {310--320},
}

Downloads: 0

{"_id":"RtQM2x8TqQwZZ88Y2","bibbaseid":"kindgren-eriksson-benedict-mohapatra-gough-hansson-kieselbach-strand-anovelproteomicapproachrevealsaroleformgprotoporphyrinixinresponsetooxidativestress-2011","author_short":["Kindgren, P.","Eriksson, M.","Benedict, C.","Mohapatra, A.","Gough, S. P.","Hansson, M.","Kieselbach, T.","Strand, Å."],"bibdata":{"bibtype":"article","type":"article","title":"A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress","volume":"141","issn":"1399-3054","url":"https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1399-3054.2010.01440.x","doi":"10/d2cw82","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.","language":"en","number":"4","urldate":"2021-09-02","journal":"Physiologia Plantarum","author":[{"propositions":[],"lastnames":["Kindgren"],"firstnames":["Peter"],"suffixes":[]},{"propositions":[],"lastnames":["Eriksson"],"firstnames":["Mats-Jerry"],"suffixes":[]},{"propositions":[],"lastnames":["Benedict"],"firstnames":["Catherine"],"suffixes":[]},{"propositions":[],"lastnames":["Mohapatra"],"firstnames":["Anasuya"],"suffixes":[]},{"propositions":[],"lastnames":["Gough"],"firstnames":["Simon","P."],"suffixes":[]},{"propositions":[],"lastnames":["Hansson"],"firstnames":["Mats"],"suffixes":[]},{"propositions":[],"lastnames":["Kieselbach"],"firstnames":["Thomas"],"suffixes":[]},{"propositions":[],"lastnames":["Strand"],"firstnames":["Åsa"],"suffixes":[]}],"year":"2011","note":"_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3054.2010.01440.x","pages":"310–320","bibtex":"@article{kindgren_novel_2011,\n\ttitle = {A novel proteomic approach reveals a role for {Mg}-protoporphyrin {IX} in response to oxidative stress},\n\tvolume = {141},\n\tissn = {1399-3054},\n\turl = {https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1399-3054.2010.01440.x},\n\tdoi = {10/d2cw82},\n\tabstract = {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.},\n\tlanguage = {en},\n\tnumber = {4},\n\turldate = {2021-09-02},\n\tjournal = {Physiologia Plantarum},\n\tauthor = {Kindgren, Peter and Eriksson, Mats-Jerry and Benedict, Catherine and Mohapatra, Anasuya and Gough, Simon P. and Hansson, Mats and Kieselbach, Thomas and Strand, Åsa},\n\tyear = {2011},\n\tnote = {\\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3054.2010.01440.x},\n\tpages = {310--320},\n}\n\n","author_short":["Kindgren, P.","Eriksson, M.","Benedict, C.","Mohapatra, A.","Gough, S. P.","Hansson, M.","Kieselbach, T.","Strand, Å."],"key":"kindgren_novel_2011","id":"kindgren_novel_2011","bibbaseid":"kindgren-eriksson-benedict-mohapatra-gough-hansson-kieselbach-strand-anovelproteomicapproachrevealsaroleformgprotoporphyrinixinresponsetooxidativestress-2011","role":"author","urls":{"Paper":"https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1399-3054.2010.01440.x"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs","fvfkWcShg3Mybjoog","Tu3jPdZyJF3j547xT"],"keywords":[],"search_terms":["novel","proteomic","approach","reveals","role","protoporphyrin","response","oxidative","stress","kindgren","eriksson","benedict","mohapatra","gough","hansson","kieselbach","strand"],"title":"A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress","year":2011}