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https://hdl.handle.net/2440/66418
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Type: | Journal article |
Title: | NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: Differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ |
Other Titles: | NMR spectroscopy of 14-3-3zeta reveals a flexible C-terminal extension: Differentiation of the chaperone and phosphoserine-binding activities of 14-3-3zeta |
Author: | Williams, D. Ecroyd, H. Goodwin, K. Dai, H. Fu, H. Woodcock, J. Zhang, L. Carver, J. |
Citation: | Biochemical Journal, 2011; 437(3):493-503 |
Publisher: | Portland Press |
Issue Date: | 2011 |
ISSN: | 0264-6021 1470-8728 |
Statement of Responsibility: | Danielle M. Williams, Heath Ecroyd, Katy L. Goodwin, Huanqin Dai, Haian Fu, Joanna M. Woodcock, Lixin Zhang and John A. Carver |
Abstract: | Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3- 3ζ isoform is a molecular chaperone, preventing the stressinduced aggregation of target proteins in a manner comparable with that of the unrelated sHsps (small heat-shock proteins). 1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3ζ and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action. Lys49 is an important functional residue within the ligand-binding groove of 14-3- 3ζ with K49E 14-3-3ζ exhibiting markedly reduced binding to phosphorylated and non-phosphorylated ligands. The R18 peptide binds to the binding groove of 14-3-3ζ with high affinity and also reduces the interaction of 14-3-3ζ ligands. However, neither the K49E mutation nor the presence of the R18 peptide affected the chaperone activity of 14-3-3ζ , implying that the C-terminal extension and binding groove of 14-3-3ζ do not mediate interaction with target proteins during chaperone action. Other region(s) in 14-3-3ζ are most likely to be involved, i.e. the protein’s chaperone and phosphoserine-binding activities are functionally and structurally separated. |
Keywords: | biophysical characterization C-terminal flexibility molecular chaperone 14-3-3 protein protein aggregation protein–protein interaction |
Rights: | © The Authors Journal compilation © 2011 Biochemical Society |
DOI: | 10.1042/BJ20102178 |
Grant ID: | ARC |
Published version: | http://dx.doi.org/10.1042/bj20102178 |
Appears in Collections: | Aurora harvest IPAS publications |
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