Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels.

ABSTRACT: The molecular chaperone HSP90 aids the maturation of a diverse but select set of metastable protein clients, many of which are key to a variety of signal transduction pathways. HSP90 function has been best investigated in animal and fungal systems, where inhibition of the chaperone has exceptionally diverse effects, ranging from reversing oncogenic transformation to preventing the acquisition of drug resistance. Inhibition of HSP90 in the model plant Arabidopsis thaliana uncovers novel morphologies dependent on normally cryptic genetic variation and increases stochastic variation inherent to developmental processes. The biochemical activity of HSP90 is strictly conserved between animals and plants. However, the substrates and pathways dependent on HSP90 in plants are poorly understood. Pro

SUBMITTER: Sangster TA 

PROVIDER: S-EPMC1920555 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature