Dimerization of Arabidopsis 14-3-3 proteins: Structural requirements within the N-terminal domain and effect of calcium

  1. Abarca, D. 1
  2. Madueño, F. 1
  3. Martínez-Zapater, J.M. 1
  4. Salinas, J. 1
  1. 1 Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria
    info

    Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria

    Madrid, España

    ROR https://ror.org/011q66e29

Revista:
FEBS Letters

ISSN: 0014-5793

Año de publicación: 1999

Volumen: 462

Número: 3

Páginas: 377-382

Tipo: Artículo

DOI: 10.1016/S0014-5793(99)01560-4 PMID: 10622729 SCOPUS: 2-s2.0-0032726938 GOOGLE SCHOLAR

Otras publicaciones en: FEBS Letters

Repositorio institucional: lock_openAcceso abierto Editor

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.