An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation

Konishi, Tenji; Ohnishi‐Kameyama, Mayumi; Funane, Kazumi; Miyazaki, Yasumasa; Konishi, Teruko; Ishii, Tadashi

doi:10.1016/j.carres.2010.01.008

Cited by 27 publications

(37 citation statements)

References 16 publications

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“…158 R was glycosylated (28), which is consistent with a previous study demonstrating that reacting sweet corn RGP with UDP-Glc results in the attachment of a single glucosyl residue to an arginyl residue (29). Thus, Arg158 likely has a role in autoglycosylation and ring interconversion.…”

Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S supporting

confidence: 90%

“…The mass of glucosylated rUAM 1 (41,414 Da) was about 159 amu higher than the mass of rUAM1 (41,255 Da), indicating that the glycosylated rUAM1 contained one hexosyl residue (28). Next, we identified the glycosylated amino acid residue(s) in the glycosylated polypeptides.…”

Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S mentioning

confidence: 96%

“…To determine if these residues are also involved in catalysis, site-directed mutagenesis was performed on the rUAMs. The results showed that the reversibly glycosylated arginyl residues are also required for catalytic ring interconversion and that Arg165 of rUAM1 and Arg163 of rUAM3 are required for mutase activity (28). UAM and all of the RGPs identified to date contain a DXD motif that is characteristic of the GT-A family of glycosyltransferases (30 OsUAM2 has no discernible mutase activity in vitro despite similarities in its amino acid sequence with both OsUAM1 and OsUAM3 (42% identity, 63% similarity).…”

Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S mentioning

confidence: 99%

“…OsUAM2 the DXD motif in UAM1 (UAM1-D112N) resulted in the loss of enzyme activity, indicating that the DDD motif itself is required for mutase activity (28). A flavin-derived iminium ion has been proposed to be involved in the interconversion of UDP-Galp and UDP-Galf catalyzed by bacterial FAD-dependent UDP-galactopyranose mutases (19,22,23).…”

Section: Figmentioning

confidence: 99%

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The Origin and Functions of Arabinofuranosyl Residues in Plant Cell Walls

Konishi

Ishii

2012

TIGG

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L-Arabinofuranosyl (Araf) residues are a quantifiably important constituent of plant cell walls. The results of earlier studies have led to the hypothesis that UDP-L-arabinopyranose (UDP-Arap) is the sugar donor and that the conversion to Araf occurs during the glycosyl transfer reaction. However, this mechanism is unlikely because UDP-L-arabinofuranose (UDP-Araf) has been shown to be the sugar donor in the conversion of Araf-containing oligosaccharides in plant extracts. We speculated that UDP-Arap reacts with a mutase to form UDP-Araf and identified and partially characterized a rice UDP-L-arabinopyranose mutase (UAM) that catalyzes the interconversion of UDP-Arap and UDP-Araf. To investigate the effects of depleting Araf residues on cell wall structure and on rice growth and development, we used RNAi to suppress UAM expression in rice plants. Several transgenic plants had reduced proportions of Araf in their cell walls together with a decrease in the extent of substitution of the xylan backbone and a reduction of between 25% and 80% in ferulic acid and p-coumaric acid content. Transgenic plants with over 25% reduction in Araf residues were dwarfed and infertile. These results suggested that Araf residues are required for normal plant growth, development, and reproduction.

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Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S supporting

confidence: 90%

Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S mentioning

confidence: 96%

Section: E An Arginyl Residue In Rice Udp-arabinopyranose M U T a S mentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

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The Origin and Functions of Arabinofuranosyl Residues in Plant Cell Walls

Konishi

Ishii

2012

TIGG

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“…After electrophoresis, the gels were stained with Bio-safe Coomassie Stain. The major bands were excised and applied to LC-ESI Mass Spectrometry (Konishi et al, 2010). Otherwise, for immunoblotting analysis, proteins were transferred to polyvinylidene difluoride (PVDF) membranes by electroblotting in Towbin buffer (Towbin et al, 1979) with a Trans-Blot Semi-Dry Transfer Cell.…”

Section: Introductionmentioning

confidence: 99%

Immunoblotting Analysis of nsLTP1 in Cereal Grains with Antiserum Raised against Recombinant Rice nsLTP1

Lang

Kagiya

Ohnishi‐Kameyama

et al. 2011

FSTR

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Nonspecific lipid transfer protein 1 (nsLTP1) is widely distributed in plants and has been recognized as a widely cross-reacting plant pan-allergen. In the present study, a recombinant protein of rice nsLTP1 was prepared with an Escherichia coli expression system, and polyclonal antiserum was raised by immunizing rabbits with this recombinant nsLTP1. The antiserum specifically immunoreacted with rice nsLTP1 and homologous nsLTP1 proteins of other kinds of cereal grains. Moreover, the antiserum was applied to compare nsLTP1 content among rice cultivars and among rice fractions separated by grain-milling. Variation of nsLTP1 contents were observed among rice cultivars, and rice nsLTP1 was proved to be mainly located in the outer layer of rice grains, providing evidence for decreasing nsLTP1 content by grain-milling.

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Coimmunoprecipitation of reversibly glycosylated polypeptide with sucrose synthase from developing castor oilseeds

et al. 2017

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The sucrose synthase (SUS) interactome of developing castor oilseeds (COS; Ricinus communis) was assessed using coimmunoprecipitation (co-IP) with anti-(COS RcSUS1)-IgG followed by proteomic analysis. A 41-kDa polypeptide (p41) that coimmunoprecipitated with RcSUS1 from COS extracts was identified as reversibly glycosylated polypeptide-1 (RcRGP1) by LC-MS/MS and anti-RcRGP1 immunoblotting. Reciprocal Far-western immunodot blotting corroborated the specific interaction between RcSUS1 and RcRGP1. Co-IP using anti-(COS RcSUS1)-IgG and clarified extracts from other developing seeds as well as cluster (proteoid) roots of white lupin and Harsh Hakea consistently recovered 90 kDa SUS polypeptides along with p41/RGP as a SUS interactor. The results suggest that SUS interacts with RGP in diverse sink tissues to channel UDP-glucose derived from imported sucrose into hemicellulose and/or glycoprotein/glycolipid biosynthesis.

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An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation

Cited by 27 publications

References 16 publications

The Origin and Functions of Arabinofuranosyl Residues in Plant Cell Walls

The Origin and Functions of Arabinofuranosyl Residues in Plant Cell Walls

Immunoblotting Analysis of nsLTP1 in Cereal Grains with Antiserum Raised against Recombinant Rice nsLTP1

Coimmunoprecipitation of reversibly glycosylated polypeptide with sucrose synthase from developing castor oilseeds

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