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Small Hsps (sHsps) and the structurally related eye lensa-crystallins are ubiquitous stress proteins that exhibit ATP-independent molecular chaperone activity. We studied thechaperone activity of dodecameric wheatTaHsp16.9C-I, aclass I cytosolic sHsp from plants and the only eukaryoticsHsp for which a high resolution structure is available,along with the related wheat proteinTaHsp17.8C-II, whichrepresents the evolutionarily distinct class II plant cytosolicsHsps. Despite the available structural information onTaHsp16.9C-I, there is minimal data on its chaperoneactivity, and likewise, data on activity of the class II pro-teins is very limited. ...
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Báo cáo khóa học: Chaperone activity of cytosolic small heat shock proteins from wheat
