The small heat shock proteins in plants are members of an ancient family of heat induced proteins

被引:0
作者
Elizabeth Vierling
机构
[1] University of Arizona,Department of Biochemistry
来源
Acta Physiologiae Plantarum | 1997年 / 19卷
关键词
molecular chaperone; thermotolerance; prokaryotes; evolution;
D O I
暂无
中图分类号
学科分类号
摘要
In response to high temperature stress, plants express numerous small heat shock proteins (sHSPs) belonging to at least five related gene families. in vitro studies suggest sHSPs act as molecular chaperones to prevent irreversible heat denaturation of other proteins. The diversity of sHSPs in plants is unique among eukaryotes and makes it of interest to understand the origins of these proteins. sHSP-related proteins have now been identified in 13 prokaryotes, and in many of these prokaryotes the sHSPs are heat-regulated as seen higher plants. The prokaryotic sHSPs were analyzed by pairwise and mutliple sequence alignments with each other and with plant sHSPs. The higher plant class I cytosolic sHSPs are shown to be most similar to a subset of the prokaryotic sHSPs, including HSP 16.6 from the cyanobacterium Synechocystis. Genetic studies in this model cyanobacterium may provide insight into sHSP function in vivo, and into potential roles of sHSPs in higher plant cells.
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页码:539 / 547
页数:8
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