The heterologous interactions among plant 14-3-3 proteins and identification of regions that are important for dimerization.
The 14-3-3 proteins constitute a family of dimeric proteins that are involved in many cellular functions. At least two mammalian 14-3-3 proteins can form heterodimers and the approximate regions important for dimerization have been identified. In this study, we demonstrate that eight Arabidopsis and one maize 14-3-3 protein can dimerize with each other and with themselves. Native gel Western analysis of Arabidopsis cell extract also suggests the presence of 14-3-3 heterodimers in vivo. Finally, we identified the domains of one 14-3-3 protein that are sufficient for homodimerization and heterodimerization. These data support the hypothesis that evolutionarily divergent 14-3-3 proteins can interact with each other to form diverse molecular modulators or adapters in signaling pathways.
Wu
K
K
Horticultural Science Department, University of Florida, Gainesville 32611, USA.
Lu
G
G
Sehnke
P
P
Ferl
R J
RJ
D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry*; D015153:Blotting, Western; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins; D012441:Saccharomyces cerevisiae; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014446:Tyrosine 3-Monooxygenase; D003313:Zea mays / Q000737:chemistry*
D048948:14-3-3 Proteins; D010940:Plant Proteins; D011506:Proteins; D011994:Recombinant Proteins; D014446:Tyrosine 3-Monooxygenase