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. Dunker, Vladimir N. Uversky

Research output: Contribution to journalArticle

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

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Intrinsically Disordered Proteins
Proteins
Molecular recognition
Degradation
Proteasome Endopeptidase Complex
Bioinformatics
Growth
Ubiquitin
gibberellic acid
Protein Domains
Computational Biology
Monoclonal Antibodies
Hormones

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. / Sun, Xiaolin; Jones, William T.; Harvey, Dawn; Edwards, Patrick J B; Pascal, Steven M.; Kirk, Christopher; Considine, Thérèse; Sheerin, David J.; Rakonjac, Jasna; Oldfield, Christopher J.; Xue, Bin; Dunker, A.; Uversky, Vladimir N.

In: Journal of Biological Chemistry, Vol. 285, No. 15, 09.04.2010, p. 11557-11571.

Research output: Contribution to journalArticle

Sun, X, Jones, WT, Harvey, D, Edwards, PJB, Pascal, SM, Kirk, C, Considine, T, Sheerin, DJ, Rakonjac, J, Oldfield, CJ, Xue, B, Dunker, A & Uversky, VN 2010, 'N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors', Journal of Biological Chemistry, vol. 285, no. 15, pp. 11557-11571. https://doi.org/10.1074/jbc.M109.027011
Sun, Xiaolin ; Jones, William T. ; Harvey, Dawn ; Edwards, Patrick J B ; Pascal, Steven M. ; Kirk, Christopher ; Considine, Thérèse ; Sheerin, David J. ; Rakonjac, Jasna ; Oldfield, Christopher J. ; Xue, Bin ; Dunker, A. ; Uversky, Vladimir N. / N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 15. pp. 11557-11571.
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AU - Sheerin, David J.

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