Dimerization of Arabidopsis 14-3-3 proteins Structural requirements within the N-terminal domain and effect of calcium
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.
| Main Authors: | , , , |
|---|---|
| Format: | journal article biblioteca |
| Language: | eng |
| Published: |
1999
|
| Online Access: | http://hdl.handle.net/20.500.12792/2073 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|