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KMID : 0368420130560010007
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Journal of Plant Biology
2013 Volume.56 No. 1 p.7 ~ p.12
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Cloning and characterization of a putative UDP-rhamnose synthase 1 from Populus euramericana Guinier
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Kim Bong-Gyu
Jung Woo-Dam
Ahn Joong-Hoon
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Abstract
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L-Rhamnose is a constituent of plant primary cell wall polysaccharides including rhamnogalacturonan-I, rhamnogalacturonan-II, and other natural plant-based compounds. UDP-rhamnose serves as a rhamnose donor whose synthesis is catalyzed by UDP-rhamnose synthase (RHM). A RHM gene, PRHM was cloned from Populus euramericana Guinier. PRHM contains two domains: the NAD dependent epimerase/dehydratase family domain and the RmlD (dTDP-keto-rhamnose-4-keto-reductase) substrate-binding domain. Because the recombinant PRHM did not demonstrate any activity during an in vitro assay, complementation with an Escherichia coli mutant was carried out. The rfbD (dTDP-4-dehydrorhamnose reductase), which encodes an enzyme catalyzing the conversion of dTDP-4-keto-rhamnose to TDP-rhamnose, was mutated in E. coli. The mutant strain B-rfbD was transformed with PRHM gene and a flavonoid rhanmosyltransferase gene, AtUGT78D1. The resulting transformant was able to convert quercetin into quercetin 3-O-rhamnoside in a manner similar to that by the wild type E. coli strain harboring AtUGT78D1. This result indicated that PRHM catalyzed the conversion of UDP-glucose into UDP-rhamnose.
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KEYWORD
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Populus euramericana, UDP-rhamnose, UDP-rhamnose synthase
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