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Dimerization of Arabidopsis 14‐3‐3 proteins: structural requirements within the N‐terminal domain and effect of calcium
Author(s) -
Abarca Dolores,
Madueño Francisco,
Martı́nez-Zapater José Miguel,
Salinas Julio
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01560-4
Subject(s) - arabidopsis , gene isoform , arabidopsis thaliana , calcium , chemistry , domain (mathematical analysis) , biochemistry , biophysics , microbiology and biotechnology , stereochemistry , biology , gene , mutant , mathematical analysis , mathematics , organic chemistry
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.