期刊
JOURNAL OF PLANT PHYSIOLOGY
卷 162, 期 2, 页码 161-168出版社
URBAN & FISCHER VERLAG
DOI: 10.1016/j.jplph.2004.09.006
关键词
sucrose-phosphate synthase; 14-3-3 protein; protein-protein interaction; yeast two-hybrid system
Sucrose-6-phosphate synthase (SPS) is a target for 14-3-3 protein binding in plants. Because several isoforms of the 14-3-3 protein are expressed in plants, I investigated which isoforms have the ability to bind SPS. Two 14-3-3 isoforms (T14-3d and a novel isoform designated T14-3 g) were found to interact with SPS from tobacco (Nicotiana tabacum L.) in a two-hybrid screen. To further address the question of isoform specificity of 14-3-3s, four additional isoforms were tested for their ability to interact with SPS in the yeast two-hybrid system. The results clearly revealed Large differences in affinity between individual 14-3-3 isoforms toward SPS. Deletion analysis suggested that these differences were mediated by the variable C-terminus of 14-3-3s. Site-directed mutagenesis of candidate 14-3-3 binding sites on SPS demonstrated that interaction could be independent of a phosphorylated serine residue within conserved binding motifs in the yeast system. These findings suggest that the Large number of 14-3-3 isoforms present in plants reflects functional specificity. (c) 2004 Elsevier GmbH. All rights reserved.
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