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The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress

Härndahl, Ulrika; Buffoni Hall, Roberta LU ; Osteryoung, K.W.; Vierling, E.; Bornman, Janet LU and Sundby, Cecilia (1999) In Cell Stress & Chaperones 4(2). p.129-138
Abstract
The nuclear-encoded chloroplast-localized Hsp21 is an oligomeric heat shock protein (Hsp), belonging to the protein family of small Hsps and @a-crystallins. We have investigated the effects of high temperature and oxidation treatments on the structural properties of Hsp21, both in purified recombinant form and in transgenicArabidopsis thalianaplants engineered to constitutively overexpress Hsp21. A conformational change was observed for the 300 kDa oligomeric Hsp21 protein during moderate heat stress (=<40oC) ofArabidopsisplants, as judged by a shift to lower mobility in non-denaturing electrophoresis. Similar changes in mobility were observed when purified recombinant Hsp21 protein was subjected to an oxidant. Exposure of Hsp21 protein... (More)
The nuclear-encoded chloroplast-localized Hsp21 is an oligomeric heat shock protein (Hsp), belonging to the protein family of small Hsps and @a-crystallins. We have investigated the effects of high temperature and oxidation treatments on the structural properties of Hsp21, both in purified recombinant form and in transgenicArabidopsis thalianaplants engineered to constitutively overexpress Hsp21. A conformational change was observed for the 300 kDa oligomeric Hsp21 protein during moderate heat stress (=<40oC) ofArabidopsisplants, as judged by a shift to lower mobility in non-denaturing electrophoresis. Similar changes in mobility were observed when purified recombinant Hsp21 protein was subjected to an oxidant. Exposure of Hsp21 protein to temperatures above 70oC led to irreversible aggregation, which was prevented in presence of the reductant dithiothreitol. The transgenic plants that constitutively overexpressed Hsp21 were more resistant to heat stress than were wildtype plants when the heat stress was imposed under high light conditions. These results suggest that the physiological role of Hsp21 involves a response to temperature-dependent oxidative stress. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cell Stress & Chaperones
volume
4
issue
2
pages
129 - 138
publisher
Churchill Livingstone
external identifiers
  • scopus:0344172562
ISSN
1466-1268
DOI
10.1379/1466-1268(1999)004<0129:TCSHSP>2.3.CO;2
language
English
LU publication?
yes
id
e41131ad-a322-4269-9893-8b050bfd1cbc (old id 125324)
date added to LUP
2007-07-05 15:02:30
date last changed
2017-06-11 04:32:01
@article{e41131ad-a322-4269-9893-8b050bfd1cbc,
  abstract     = {The nuclear-encoded chloroplast-localized Hsp21 is an oligomeric heat shock protein (Hsp), belonging to the protein family of small Hsps and @a-crystallins. We have investigated the effects of high temperature and oxidation treatments on the structural properties of Hsp21, both in purified recombinant form and in transgenicArabidopsis thalianaplants engineered to constitutively overexpress Hsp21. A conformational change was observed for the 300 kDa oligomeric Hsp21 protein during moderate heat stress (=&lt;40oC) ofArabidopsisplants, as judged by a shift to lower mobility in non-denaturing electrophoresis. Similar changes in mobility were observed when purified recombinant Hsp21 protein was subjected to an oxidant. Exposure of Hsp21 protein to temperatures above 70oC led to irreversible aggregation, which was prevented in presence of the reductant dithiothreitol. The transgenic plants that constitutively overexpressed Hsp21 were more resistant to heat stress than were wildtype plants when the heat stress was imposed under high light conditions. These results suggest that the physiological role of Hsp21 involves a response to temperature-dependent oxidative stress.},
  author       = {Härndahl, Ulrika and Buffoni Hall, Roberta and Osteryoung, K.W. and Vierling, E. and Bornman, Janet and Sundby, Cecilia},
  issn         = {1466-1268},
  language     = {eng},
  number       = {2},
  pages        = {129--138},
  publisher    = {Churchill Livingstone},
  series       = {Cell Stress & Chaperones},
  title        = {The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress},
  url          = {http://dx.doi.org/10.1379/1466-1268(1999)004<0129:TCSHSP>2.3.CO;2},
  volume       = {4},
  year         = {1999},
}