478701-11-0Relevant articles and documents
Detection of 210 kDa receptor protein for a leaf-movement factor by using novel photoaffinity probes
Fujii, Tomohiko,Manabe, Yoshiyuki,Sugimoto, Takanori,Ueda, Minoru
, p. 7874 - 7893 (2007/10/03)
Circadian rhythmic plant leaf-movement, called nyctinasty, is controlled by a time-course change in the internal concentration of the leaf-movement factor in the plant body. We revealed that specific binding proteins (210 and 180 kDa) for the leaf-movement factor, potassium lespedezate (1), are contained in the plasma membrane of the plant motor cell by using novel synthetic photoaffinity probes. These proteins are localized on the motor cell in the plant body, and would be potential receptors for the leaf-movement factor to control the leaf-movement. Our study is a rare successful result of the detection of membrane receptors by using a synthetic photoaffinity probe designed on a biologically active natural product. And these results also advance a guideline for probe design towards successful photoaffinity labeling.
Syntheses of novel photoaffinity probes for bioorganic studies on nyctinasty of leguminous plants
Sugimoto, Takanori,Fujii, Tomohiko,Hatanaka, Yasumaru,Yamamura, Shosuke,Ueda, Minoru
, p. 6529 - 6532 (2007/10/03)
Novel and non-radioactive photoaffinity probes (1 and 2) for the bioorganic study of nyctinasty are designed and synthesized based on potassium isolespedezate (3), which induce leaf-opening against the leaf of Cassia mimosoides L. These probes bear a trifluoromethyldiazirine or diazophenyl group for photoaffinity and a biotin subunit for affinity chromatography and chemiluminescent detection. Probes (1 and 2) showed leaf-opening activity at 5×10-5 mol/L with leaves of C. mimosoides; thus, they would be an important tool for the identification of a receptor protein for 3.