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. Pascal, Christopher Kirk, Thérèse Considine, David J. Sheerin, Jasna Rakonjac, Christopher J. Oldfield, Bin Xue, A. Keith Dunker, Vladimir N. Uversky

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Abstract

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 unbound N-terminal domains of DELLAs are intrinsically unstructured proteins under physiological conditions. With in the intrinsically disordered N-terminal domain of DELLAs, we have identified several molecular recognition features, sequences known to undergo disorder-to-order transitions upon binding to interacting proteins in intrinsically unstructured proteins. In accordance with the molecular recognition feature analyses, we have observed the binding-induced folding of N-terminal domains of DELLAs upon interaction with AtGID1/GA. Our results also indicate that DELLA proteins can be divided into two subgroups in terms of their molecular compactness and their interactions with monoclonal antibodies.

Original languageEnglish (US)
Pages (from-to)11557-11571
Number of pages15
JournalJournal of Biological Chemistry
Volume285
Issue number15
DOIs
StatePublished - Apr 9 2010

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sun, X., Jones, W. T., Harvey, D., Edwards, P. J. B., Pascal, S. M., Kirk, C., Considine, T., Sheerin, D. J., Rakonjac, J., Oldfield, C. J., Xue, B., Dunker, A. K., & Uversky, V. N. (2010). N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. Journal of Biological Chemistry, 285(15), 11557-11571. https://doi.org/10.1074/jbc.M109.027011