Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Homodimer. Most abundantly expressed in roots and apical shoots. Low expression in mature leaves. Increasing levels of expression observed in developing ovaries, floral shoots and roots. Levels decrease with maturation. Heat treatment increases expression 3-fold in mature leaves. Has little effect on developing shoot apices. The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins. Belongs to the heat shock protein 90 family.