Small Hsps (sHsps) and the structurally related eye lens a-crystallins are ubiquitous stress proteins that exhibit ATP-independent molecular chaperone activity. We studied the chaperone activity of dodecameric , a class I cytosolic sHsp from plants and the only eukaryotic sHsp for which a high resolution structure is available, along with the related wheat , which represents the evolutionarily distinct class II plant cytosolic sHsps. Despite the available structural information on , there is minimal data on its chaperone activity, and likewise, data on activity of the class II pro-teins is very limited. .
