Linked Life Data

21158868

Source:http://linkedlifedata.com/resource/pubmed/id/21158868

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-3-8
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1399-3054
pubmed:author
pubmed:copyrightInfo
Copyright © Physiologia Plantarum 2011.
pubmed:issnType
Electronic
pubmed:volume
141
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
310-20
pubmed:meshHeading
pubmed-meshheading:21158868-Amino Acid Motifs, pubmed-meshheading:21158868-Arabidopsis, pubmed-meshheading:21158868-Arabidopsis Proteins, pubmed-meshheading:21158868-Blotting, Western, pubmed-meshheading:21158868-Computational Biology, pubmed-meshheading:21158868-Gene Expression Regulation, Plant, pubmed-meshheading:21158868-Light-Harvesting Protein Complexes, pubmed-meshheading:21158868-Lyases, pubmed-meshheading:21158868-Oxidative Stress, pubmed-meshheading:21158868-Protein Binding, pubmed-meshheading:21158868-Protein Subunits, pubmed-meshheading:21158868-Proteomics, pubmed-meshheading:21158868-Protoporphyrins, pubmed-meshheading:21158868-Reproducibility of Results, pubmed-meshheading:21158868-Signal Transduction, pubmed-meshheading:21158868-Spectrometry, Fluorescence, pubmed-meshheading:21158868-Stress, Physiological, pubmed-meshheading:21158868-Tetrapyrroles
pubmed:year
2011
pubmed:articleTitle
A novel proteomic approach reveals a role for Mg-protoporphyrin IX in response to oxidative stress.
pubmed:affiliation
Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, SE-901 87 Umeå, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't