Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Gustavsson, Niklas LU ; Härndal, Ulrika ; Gisselsson, Anna LU ; Ruepstorff, Peter and Sundby, Cecilia (1999) In Protein Science 8(11). p.2506-2512
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Protein Science
volume
8
issue
11
pages
2506 - 2512
publisher
The Protein Society
external identifiers
  • scopus:0345009031
ISSN
1469-896X
DOI
10.1110/ps.8.11.2506
language
English
LU publication?
yes
id
00de9101-2034-425b-8a10-e7c7f3c95579 (old id 125294)
date added to LUP
2016-04-01 11:33:32
date last changed
2025-04-04 15:33:02
@article{00de9101-2034-425b-8a10-e7c7f3c95579,
  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.}},
  author       = {{Gustavsson, Niklas and Härndal, Ulrika and Gisselsson, Anna and Ruepstorff, Peter and Sundby, Cecilia}},
  issn         = {{1469-896X}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{2506--2512}},
  publisher    = {{The Protein Society}},
  series       = {{Protein Science}},
  title        = {{Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer}},
  url          = {{http://dx.doi.org/10.1110/ps.8.11.2506}},
  doi          = {{10.1110/ps.8.11.2506}},
  volume       = {{8}},
  year         = {{1999}},
}