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Título: | Structural transitions in orb2 prion-like domain relevant for functional aggregation in memory consolidation |
Autor: | Oroz, Javier CSIC ORCID; Félix, Sara S.; Cabrita, E.J.; Laurents, Douglas V. CSIC ORCID | Fecha de publicación: | 22-oct-2020 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 295: 18122-18133 (2020) | Resumen: | The recent structural elucidation of ex vivo Drosophila Orb2 fibrils revealed a novel amyloid formed by interdigitated Gln and His residue side chains belonging to the prion-like domain. However, atomic-level details on the conformational transitions associated with memory consolidation remain unknown. Here, we have characterized the nascent conformation and dynamics of the prion-like domain (PLD) of Orb2A using a nonconventional liquid-state NMR spectroscopy strategy based on C detection to afford an essentially complete set of Ca, Cb, Ha, and backbone CO and N assignments. At pH 4, where His residues are protonated, the PLD is disordered and flexible, except for a partially populated a-helix spanning residues 55–60, and binds RNA oligos, but not divalent cations. At pH 7, in contrast, His residues are predominantly neutral, and the Q/H segments adopt minor populations of helical structure, show decreased mobility and start to self-associate. At pH 7, the His residues do not bind RNA or Ca, but do bind Zn, which promotes further association. These findings represent a remarkable case of structural plasticity, based on which an updated model for Orb2A functional amyloidogenesis is suggested. | Descripción: | 12 pags., 5 figs. | Versión del editor: | http://dx.doi.org/10.1074/jbc.RA120.015211 | URI: | http://hdl.handle.net/10261/229400 | DOI: | 10.1074/jbc.RA120.015211 | Identificadores: | doi: 10.1074/jbc.RA120.015211 issn: 1083-351X |
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Structural transitions.pdf | 3,32 MB | Adobe PDF | Visualizar/Abrir |
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