| Literature DB >> 10622729 |
D Abarca1, F Madueño, J M Martínez-Zapater, J Salinas.
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.Entities:
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Year: 1999 PMID: 10622729 DOI: 10.1016/s0014-5793(99)01560-4
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124