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.
Abarca
D
D
Departamento de Mejora Genética y Biotecnología, INIA, Madrid, Spain.
Madueño
F
F
Martínez-Zapater
J M
JM
Salinas
J
J
D048948:14-3-3 Proteins; D017360:Arabidopsis / Q000737:chemistry*; D002118:Calcium / Q000494:pharmacology*; D002122:Calcium Chloride / Q000494:pharmacology; D019281:Dimerization; D005982:Glutathione Transferase / Q000378:metabolism; D015636:Magnesium Chloride / Q000494:pharmacology; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D020033:Protein Isoforms; D011506:Proteins / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D010455:Peptides; D020033:Protein Isoforms; D011506:Proteins; D011993:Recombinant Fusion Proteins; D015636:Magnesium Chloride; D014446:Tyrosine 3-Monooxygenase; D005982:Glutathione Transferase; D002122:Calcium Chloride; D002118:Calcium