Submitted to: Journal of the American Chemical Society
Publication Type: Peer reviewed journal
Publication Acceptance Date: 12/31/2004
Publication Date: 6/30/2005
Citation: Nyangulu, J.M., Galka, M.M., Jadhav, A., Gai, Y., Graham, C.M., Nelson, K.M., Cutler, A.J., Taylor, D.C., Banowetz, G.M., Abrams, S.R. 2005. Affinity probes for isolation of abscisic acid-binding proteins. Journal of the American Chemical Society. v.127. p.1662-1664. Interpretive Summary: The plant hormone, abscisic acid (ABA) regulated many agronomically important process during the development of many crop plants including seed formation and responses to environmental stresses. The mechanism by which ABA binds to plant components to participate in these physiological processes remains unknown. This study developed a probe to isolate plant proteins capable of binding ABA so that further progress can be made in understanding the pathways by which ABA interacts with plant components to impact stress tolerance and plant development.
Technical Abstract: An affinity-based method that employed a biologically active derivative of abscisic acid (ABA) linked to Sepharose was developed for isolation of ABA-binding proteins from plant extracts. The receptor probe incorporated all the functional groups of ABA required for binding to an anti-(+)-ABA monoclonal antibody including stereochemistry at C-1, the acid functional group on the side chain, and the ketone on the ring. The synthesis of the bioactive, biotinylated probe is described and validation of the probe was provided by isolation of ABA-8'hydroxylase.