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N-Terminal Domains Of Della Proteins Are Intrinsically Unstructured In The Absence Of Interaction With Gid1/Gibberellic Acid Receptors, Xiaolin Sun, William T. Jones, Dawn Harvey, Patrick J. B. Edwards, Steven M. Pascale, Christopher Kirk, Thérèse Considine, David J. Sheerin, Jasna Rakonjac, Christopher J. Oldfield, Bin Xue, A. Keith Dunker, Vladimir N. Uversky

Molecular Medicine Faculty Publications

The plant growth-repressing DELLA proteins (DELLAs) are known to represent a convergence point in integration of multiple developmental and environmental signals in planta, one of which is hormone gibberellic acid (GA). Binding of the liganded GA receptor (GID1/GA) to the N-terminal domain of DELLAs is required for GA-induced degradation of DELLAs via the ubiquitin-proteasome pathway, thus derepressing plant growth. However, the conformational changes of DELLAs upon binding to GID1/GA, which are the key to understanding the precise mechanism of GID1/GA-mediated degradation of DELLAs, remain unclear. Using biophysical, biochemical, and bioinformatics approaches, we demonstrated for the first time that the …