Document Type
Article
Publication Date
2010
Keywords
Organisms, Plant Protein, Protein-protein Interactions, Protein/folding, Signal Transduction, Biophysics, Della Proteins, Ga Signaling, Gid1 Receptor, Binding-induced Folding, Intrinsically Unstructured Proteins
Digital Object Identifier (DOI)
https://doi.org/10.1074/jbc.M109.027011
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. Within 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.
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. Within 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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Biological Chemistry, v. 285, issue 15, p. 11557-11571
Scholar Commons Citation
Sun, Xiaolin; Jones, William T.; Harvey, Dawn; Edwards, Patrick J. B.; Pascale, Steven M.; Kirk, Christopher; Considine, Thérèse; Sheerin, David J.; Rakonjac, Jasna; Oldfield, Christopher J.; Xue, Bin; Dunker, A. Keith; and Uversky, Vladimir N., "N-terminal Domains of DELLA Proteins Are Intrinsically Unstructured in The Absence of Interaction with Gid1/gibberellic Acid Receptors" (2010). Molecular Medicine Faculty Publications. 550.
https://digitalcommons.usf.edu/mme_facpub/550
