ArticleProtein science : a publication of the Protein Society1999
Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 34 citations in OpenAlex.
- Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study ofPlants (Basel, Switzerland) · 2022Article
- Mass spectrometric analysis of differentially expressed proteins in an endangered medicinal herb, Picrorhiza kurroa.BioMed research international · 2014Article
- Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase.Protein science : a publication of the Protein Society · 2007Article
- Divergent evolution of the chloroplast small heat shock protein gene in the genera Rhododendron (Ericaceae) and Machilus (Lauraceae).Annals of botany · 2007Article
- Investigations into the role of the plastidial peptide methionine sulfoxide reductase in response to oxidative stress in Arabidopsis.Plant physiology · 2004Article
- Sulfur assimilation and the role of sulfur in plant metabolism: a survey.Photosynthesis research · 2004Article
- Heat sensitivity in a bentgrass variant. Failure to accumulate a chloroplast heat shock protein isoform implicated in heat tolerance.Plant physiology · 2003Article
- Oxidative stress and acclimation mechanisms in plants.The arabidopsis book · 2002Article
- Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox-response but retained chaperone-like activity.Protein science : a publication of the Protein Society · 2001Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The small heat shock proteins (sHsps), which counteract heat and oxidative stress in an unknown way, belong to a protein family of sHsps and alpha-crystallins whose members form large oligomeric complexes. The chloroplast-localized sHsp, Hsp21, contains a conserved methionine-rich sequence, predicted to form an amphipatic helix with the methionines situated along one of its sides. Here, we report how methionine sulfoxidation was detected by mass spectrometry in proteolytically cleaved peptides that were produced from recombinant Arabidopsis thaliana Hsp21, which had been treated with varying concentrations of hydrogen peroxide. Sulfoxidation of the methionine residues in the conserved amphipatic helix coincided with a significant conformational change in the Hsp21 protein oligomer.
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