A Nicotiana plumbaginifolia protein labeled with an
azido cytokinin agonist is a glutathione S-
五点法transferase届时光临>ELECTRONICSWORKBENCH
期刊名称： Physiologia Plantarum
作者： Gonneau, Martine,Mornet, René,Laloue, Michel
11眼
皮黔生年份： 2010年
期号： 第1期电子商务与电子政务
关键词： Cytokinin;cytokinin‐binding;glutathione S‐transferase;Nicotiana
plumbaginifolia;photoaffinity labeling
摘要：The mechanisms of reception/transduction of cytokinins still remain
largely unknown. We used 1‐(2‐azido‐6‐chloropyrid‐4‐yl)‐3‐(4‐[ 3 H])phenylurea ([ 3 H]azido‐CPPU), a new photoaffinity probe to search for cytokinin‐binding proteins.
A soluble protein that binds phenylurea‐type cytokinins has been specifically photolabeled in Nicotiana plumbaginifolia (cv. Viviani line pbH1D) leaf extracts. The protein was purified to homogeneity by affinity chromatography. Its N‐terminal amino acid sequence, as well as four internal peptidic sequences are highly homologous with the theta class of the glutathione S‐transferase superfamily (GST, EC 2.5.1.18) including Hyoscyamus muticus and Arabidopsis GSTs identified as auxin‐binding proteins. The purified N. plumbaginifolia protein also possesses GST enzymatic activity. To...
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