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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/42786
Title: Dimerization of Arabidopsis 14-3-3 proteins: structural requirements within the N-terminal domain and effect of calcium
Authors: Abarca, Dolores; Madueño, Francisco; Martínez-Zapater, José M.; Salinas, Julio
Keywords: 14-3-3 protein
Protein dimerization
Issue Date: 3-Dec-1999
Publisher: Elsevier
Citation: FEBS Letters 462(3): 377-382 (1999)
Abstract: The structural requirements for dimerization of RCI14A and RCI14B, two 14-3-3 isoforms from Arabidopsis thaliana, have been analyzed by testing truncated forms of RCI14A for dimerization with full-length RCI14A and RCI14B. The results show that only the fourth helix of the truncated partner is essential for dimerization, which represents a difference from what is known for animal isoforms. On the other hand, the effect of calcium has been tested in RCI14A homodimerization. Millimolar concentrations of calcium exert a negative, dose-dependent effect that involves the C-terminal domain of RCI14A and might modulate interactions with other cellular components or among Arabidopsis 14-3-3 isoforms.
Publisher version (URL): http://dx.doi.org/10.1016/S0014-5793(99)01560-4
URI: http://hdl.handle.net/10261/42786
ISSN: 0014-5793
DOI: 10.1016/S0014-5793(99)01560-4
E-ISSN: 1873-3468
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