SeeDev-binary@ldeleger:SeeDev-binary-14701918-4 JSONTXT

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data support the hypothesis that MUM4 encodes an enzyme involved in RGI biosynthesis. First, analysis of mum4 mucilage using antibodies and gas chromatography have demonstrated a significant reduction in RGI and its composite backbone\nmonosaccharides Rha and GalUA in comparison with wild-type seeds. Second, cloning of MUM4 revealed a putative protein containing similarity to bacterial nucleotide sugar interconversion enzymes, suggesting that\nit, too, is required for the production of activated sugars. The N-terminal portion of MUM4 is most similar to bacterial dTDP-d-Glc 4,6-dehydratases, the first of three enzymes required for the conversion of dTDP-d-Glc to dTDP-l-Rha (Tonetti et al., 1998). These data favor a role for MUM4 in the synthesis of NDP-l-Rha, a key step in the production of RGI. A reverse genetics approach taken by another group has come to a similar conclusion\nregarding the putative enzymatic function of MUM4 (also designated RHM2 [RHAMNOSE BIOSYNTHESIS 2]; B. Usadel et al., 2004). However, another role in RGI biosynthesis cannot be ruled out without evidence of enzymatic activity in the conversion\nof NDP-d-Glc to NDP-l-Rha.\nGram-negative bacteria such as Escherichia coli encode three separate enzymes (4,6-dehydratase, 3,5-epimerase, and 4-reductase) to convert dTDP-d-Glc to dTDP-l-Rha (Tonetti et al., 1998). The putative MUM4 protein not only contains an N-terminal domain with similarity to the bacterial dTDP-d-Glc 4,6-dehydratases but also a C-terminal domain with some similarity to 4-reductases (this study; Reiter and Vanzin, 2001). There is a precedent in Arabidopsis for a bifunctional 3,5 epimerase, 4-reductase in the synthesis of GDP-l-Fuc from GDP-d-Man (GER1, GER2) (Bonin and Reiter, 2000). Therefore, based on sequence analysis, it is attractive to postulate a single, multifunctional protein acting in the conversion\nof NDP-d-Glc to NDP-l-Rha in Arabidopsis (Reiter and Vanzin, 2001).\nMUM4 is a member of a small gene family consisting of three genes (RHM1, MUM4/RHM2, and RHM3; Reiter and Vanzin, 2001) that exhibit high identity at both nucleotide and amino acid levels. The ubiquitous expression of RHM1 and RHM3 can be postulated to provide a mechanism for the formation of the normal primary cell wall in mum4 mutants and the residual mucilage present in mum4 seed coats. Redundancy in genes coding for putative NDP-l-Rha synthases is unsurprising because of the importance of the Rha-containing pectins RGI and RGII in primary cell walls.\nIn fact, the presence of multiple genes coding enzymes involved in nucleotide sugar interconversions is common in plants (Reiter and Vanzin, 2001).\n"}