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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Peter Robert Kindgren
  • Mats-Jerry Eriksson
  • Catherine Benedict
  • Anasuya Mohapatra
  • Simon P Gough
  • Mats Hansson
  • Thomas Kieselbach
  • Asa Strand

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.

OriginalsprogEngelsk
TidsskriftPhysiologia Plantarum
Vol/bind141
Udgave nummer4
Sider (fra-til)310-20
Antal sider11
ISSN0031-9317
DOI
StatusUdgivet - 2011
Eksternt udgivetJa

ID: 183163908