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Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer

Published online by Cambridge University Press:  01 November 1999

NIKLAS GUSTAVSSON ,
ULRIKA HÄRNDAHL ,
ANNA EMANUELSSON ,
PETER ROEPSTORFF  and
CECILIA SUNDBY
NIKLAS GUSTAVSSON
Affiliation:
Department of Biochemistry, Lund University, P.O. Box 124, S-221 00 Lund, Sweden
ULRIKA HÄRNDAHL
Affiliation:
Department of Biochemistry, Lund University, P.O. Box 124, S-221 00 Lund, Sweden
ANNA EMANUELSSON
Affiliation:
Department of Plant Biochemistry, Lund University, P.O. Box 124, S-221 00 Lund, Sweden
PETER ROEPSTORFF
Affiliation:
Department of Molecular Biology, Odense University, DK 5230 Odense M, Denmark
CECILIA SUNDBY
Affiliation:
Department of Biochemistry, Lund University, P.O. Box 124, S-221 00 Lund, Sweden
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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 α-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.

Keywords

heat shock proteinheat stressmass spectrometryoxidative stresspost-translational modification
Type
Research Article
Information
Protein Science , Volume 8 , Issue 11 , November 1999 , pp. 2506 - 2512
Copyright
© 1999 The Protein Society

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