Dimerization of Arabidopsis 14-3-3 proteins: Structural requirements within the N-terminal domain and effect of calcium
- Abarca, D. 1
- Madueño, F. 1
- Martínez-Zapater, J.M. 1
- Salinas, J. 1
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1
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria
info
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria
Madrid, España
ISSN: 0014-5793
Año de publicación: 1999
Volumen: 462
Número: 3
Páginas: 377-382
Tipo: Artículo
Otras publicaciones en: FEBS Letters
Resumen
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. Copyright (C) 1999 Federation of European Biochemical Societies.