tailieunhanh - Báo cáo khoa học: Biochemical characterization of rice trehalose-6-phosphate phosphatases supports distinctive functions of these plant enzymes

Substantial levels of trehalose accumulate in bacteria, fungi, and inverte-brates, where it serves as a storage carbohydrate or as a protectant against environmental stresses. In higher plants, trehalose is detected at fairly low levels; therefore, a regulatory or signaling function has been proposed for this molecule. | ễFEBS Journal Biochemical characterization of rice trehalose-6-phosphate phosphatases supports distinctive functions of these plant enzymes Shuhei Shima1 2 Hirokazu Matsui2 Satoshi Tahara2 and Ryozo Imai1 1 Crop Cold Tolerance Research Team NationalAgriculturalResearch Center for Hokkaido Region NARO Toyohira-ku Sapporo Japan 2 Department of Applied Bioscience Graduate Schoolof Agriculture Hokkaido University Sapporo Japan Keywords functional analysis kinetic analysis Oryza sativa recombinant protein trehalose Correspondence R. Imai Crop Cold Tolerance Research Team NationalAgriculturalResearch Center for Hokkaido Region NationalAgriculture and Food Research Organization Hitsujigaoka 1 Toyohira-ku Sapporo 0628555 Japan Fax Tel 81 11 857 9382 E-mail rzi@ Received 8 November 2006 revised 14 December 2006 accepted 19 December 2006 doi Substantial levels of trehalose accumulate in bacteria fungi and invertebrates where it serves as a storage carbohydrate or as a protectant against environmental stresses. In higher plants trehalose is detected at fairly low levels therefore a regulatory or signaling function has been proposed for this molecule. In many organisms trehalose-6-phosphate phosphatase is the enzyme governing the final step of trehalose biosynthesis. Here we report that OsTPPl and OsTPP2 are the two major trehalose-6-phosphate phosphatase genes expressed in vegetative tissues of rice. Similar to results obtained from our previous OsTPP1 study complementation analysis of a yeast trehalose-6-phosphate phosphatase mutant and activity measurement of the recombinant protein demonstrated that OsTPP2 encodes a functional trehalose-6-phosphate phosphatase enzyme. OsTPP2 expression is transiently induced in response to chilling and other abiotic stresses. Enzymatic characterization of recombinant OsTPP1 and OsTPP2 revealed stringent substrate specificity for trehalose 6-phosphate and about 10 times lower Km values for .

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