메뉴 건너뛰기




Volumn 11, Issue 3, 2008, Pages 236-243

Biochemical genetics of nucleotide sugar interconversion reactions

Author keywords

[No Author keywords available]

Indexed keywords

EPIMERASE; NUCLEOTIDE; OXIDOREDUCTASE; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 44149116169     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2008.03.009     Document Type: Review
Times cited : (108)

References (53)
  • 2
    • 0034863672 scopus 로고    scopus 로고
    • Molecular genetics of nucleotide sugar interconversion pathways in plants
    • Reiter W.D., and Vanzin G.F. Molecular genetics of nucleotide sugar interconversion pathways in plants. Plant Mol Biol 47 (2001) 95-113
    • (2001) Plant Mol Biol , vol.47 , pp. 95-113
    • Reiter, W.D.1    Vanzin, G.F.2
  • 3
    • 2442434678 scopus 로고    scopus 로고
    • Nucleotide sugar interconversions and cell wall biosynthesis: how to bring the inside to the outside
    • Seifert G.J. Nucleotide sugar interconversions and cell wall biosynthesis: how to bring the inside to the outside. Curr Opin Plant Biol 7 (2004) 277-284
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 277-284
    • Seifert, G.J.1
  • 4
    • 2442610818 scopus 로고    scopus 로고
    • Glycosyltransferases and cell wall biosynthesis: novel players and insights
    • Scheible W.-R., and Pauly M. Glycosyltransferases and cell wall biosynthesis: novel players and insights. Curr Opin Plant Biol 7 (2004) 285-295
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 285-295
    • Scheible, W.-R.1    Pauly, M.2
  • 6
    • 33745188487 scopus 로고    scopus 로고
    • Distinct properties of the five UDP-d-glucose/UDP-d-galactose 4-epimerase isoforms of Arabidopsis thaliana
    • + cofactors and kinetic parameters. Light scattering and gel filtration experiments suggested that each isoform exists as a dimer in vitro. Based on results from yeast two-hybrid analyses, all isoforms are able to interact with each other suggesting that mixed dimers or higher multimers may form under in vivo conditions.
    • + cofactors and kinetic parameters. Light scattering and gel filtration experiments suggested that each isoform exists as a dimer in vitro. Based on results from yeast two-hybrid analyses, all isoforms are able to interact with each other suggesting that mixed dimers or higher multimers may form under in vivo conditions.
    • (2006) J Biol Chem , vol.281 , pp. 17276-17285
    • Barber, C.1    Rösti, J.2    Rawat, A.3    Findlay, K.4    Roberts, K.5    Seifert, G.J.6
  • 7
    • 34347405057 scopus 로고    scopus 로고
    • UDP-Glucose 4-epimerase isoforms UGE2 and UGE4 cooperate in providing UDP-galactose for cell wall biosynthesis and growth of Arabidopsis thaliana
    • A thorough phenotypic analysis of single, double, triple and quadruple mutants within the UGE gene family of Arabidopsis was performed. Mutations in single isoforms did not lead to obvious phenotypes except in case of uge4 plants which produced abnormal root hairs in agreement with previous studies. Plants with mutations in more than one isoform showed phenotypes such as deformed roots, chlorosis, poor plant growth and male sterility depending on the combination of mutant loci. Plants with UGE2 as the only functional isoform were vigorous and fertile with relatively minor growth defects. On the other hand, plants with UGE3 as the only functional isoform were galactose auxotrophs that showed major growth defects even when exogenous galactose was provided. The results from this study suggests that the various UGE isoforms acquired specialized functions during evolution even though they catalyze a freely reversible enzymatic reaction that is not expected to be tightly regulated.
    • Rösti J., Barton C.J., Albrecht S., Dupree P., Pauly M., Findlay K., Roberts K., and Seifert G.J. UDP-Glucose 4-epimerase isoforms UGE2 and UGE4 cooperate in providing UDP-galactose for cell wall biosynthesis and growth of Arabidopsis thaliana. Plant Cell 19 (2007) 1565-1579. A thorough phenotypic analysis of single, double, triple and quadruple mutants within the UGE gene family of Arabidopsis was performed. Mutations in single isoforms did not lead to obvious phenotypes except in case of uge4 plants which produced abnormal root hairs in agreement with previous studies. Plants with mutations in more than one isoform showed phenotypes such as deformed roots, chlorosis, poor plant growth and male sterility depending on the combination of mutant loci. Plants with UGE2 as the only functional isoform were vigorous and fertile with relatively minor growth defects. On the other hand, plants with UGE3 as the only functional isoform were galactose auxotrophs that showed major growth defects even when exogenous galactose was provided. The results from this study suggests that the various UGE isoforms acquired specialized functions during evolution even though they catalyze a freely reversible enzymatic reaction that is not expected to be tightly regulated.
    • (2007) Plant Cell , vol.19 , pp. 1565-1579
    • Rösti, J.1    Barton, C.J.2    Albrecht, S.3    Dupree, P.4    Pauly, M.5    Findlay, K.6    Roberts, K.7    Seifert, G.J.8
  • 8
    • 32944477384 scopus 로고    scopus 로고
    • Gene expression patterns and catalytic properties of UDP-d-glucose 4-epimerases from barley (Hordeum vulgare L.)
    • Zhang Q., Hrmova M., Shirley N.J., Lahnstein J., and Fincher G.B. Gene expression patterns and catalytic properties of UDP-d-glucose 4-epimerases from barley (Hordeum vulgare L.). Biochem J 394 (2006) 115-124
    • (2006) Biochem J , vol.394 , pp. 115-124
    • Zhang, Q.1    Hrmova, M.2    Shirley, N.J.3    Lahnstein, J.4    Fincher, G.B.5
  • 9
    • 0036909251 scopus 로고    scopus 로고
    • Functional characterization of recombinant UDP-glucose dehydrogenase from soybean
    • Hinterberg B., Klos C., and Tenhaken R. Functional characterization of recombinant UDP-glucose dehydrogenase from soybean. Plant Physiol Biochem 40 (2002) 1011-1017
    • (2002) Plant Physiol Biochem , vol.40 , pp. 1011-1017
    • Hinterberg, B.1    Klos, C.2    Tenhaken, R.3
  • 10
    • 36849006993 scopus 로고    scopus 로고
    • Genome-wide analysis of the UDP-glucose dehydrogenase gene family in Arabidopsis, a key enzyme for matrix polysaccharides in cell walls
    • + was also accepted with an approximately five-fold lower efficiency.
    • + was also accepted with an approximately five-fold lower efficiency.
    • (2007) J Exp Bot , vol.58 , pp. 3609-3621
    • Klinghammer, M.1    Tenhaken, R.2
  • 11
    • 0036918914 scopus 로고    scopus 로고
    • Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms
    • Harper A.D., and Bar-Peled M. Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms. Plant Physiol 130 (2002) 2188-2198
    • (2002) Plant Physiol , vol.130 , pp. 2188-2198
    • Harper, A.D.1    Bar-Peled, M.2
  • 12
    • 20444377995 scopus 로고    scopus 로고
    • Biosynthesis of UDP-xylose: characterization of membrane-bound AtUXS2
    • Pattathil S., Harper A.D., and Bar-Peled M. Biosynthesis of UDP-xylose: characterization of membrane-bound AtUXS2. Planta 221 (2005) 538-548
    • (2005) Planta , vol.221 , pp. 538-548
    • Pattathil, S.1    Harper, A.D.2    Bar-Peled, M.3
  • 13
    • 0002986778 scopus 로고    scopus 로고
    • The cell wall
    • Buchanan B.B., Gruissem W., and Jones R.L. (Eds), American Society of Plant Physiologists, Rockville, MD
    • Carpita N., and McCann M. The cell wall. In: Buchanan B.B., Gruissem W., and Jones R.L. (Eds). Biochemistry and Molecular Biology of Plants (2000), American Society of Plant Physiologists, Rockville, MD 52-108
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 52-108
    • Carpita, N.1    McCann, M.2
  • 14
    • 13844306333 scopus 로고    scopus 로고
    • Expression of cellulose synthase-like (Csl) genes in insect cells reveals that CslA family members encode mannan synthases
    • Liepman A.H., Wilkerson C.G., and Keegstra K. Expression of cellulose synthase-like (Csl) genes in insect cells reveals that CslA family members encode mannan synthases. Proc Natl Acad Sci U S A 102 (2005) 2221-2226
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2221-2226
    • Liepman, A.H.1    Wilkerson, C.G.2    Keegstra, K.3
  • 15
    • 0031728483 scopus 로고    scopus 로고
    • Uridine-5′-diphosphate dehydrogenase from soybean nodules
    • Stewart D.C., and Copeland L. Uridine-5′-diphosphate dehydrogenase from soybean nodules. Plant Physiol 116 (1998) 349-355
    • (1998) Plant Physiol , vol.116 , pp. 349-355
    • Stewart, D.C.1    Copeland, L.2
  • 16
    • 35148858816 scopus 로고    scopus 로고
    • Radioisotope ratios discriminate between competing pathways of cell wall polysaccharide and RNA biosynthesis in living plant cells
    • 14C]d-fructose was conducted to evaluate the relative contributions of known or postulated pathways toward the synthesis of UDP-GlcA, UDP-GalA and GDP-Glc. The two-labeled compounds enter nucleotide sugar interconversion pathways at widely separated points via salvage pathways (galactokinase and hexokinase, respectively), which permits an evaluation of the major routes toward the synthesis of specific nucleotide sugars. The overall conclusion of this study is that UDP-GlcA is primarily synthesized via oxidation of UDP-Glc to UDP-GlcA, UDP-GalA is primarily synthesized via 4-epimerization of UDP-GlcA, and GDP-Glc is primarily synthesized by guanylyl transfer from GTP onto glucose-1-phosphate.
    • 14C]d-fructose was conducted to evaluate the relative contributions of known or postulated pathways toward the synthesis of UDP-GlcA, UDP-GalA and GDP-Glc. The two-labeled compounds enter nucleotide sugar interconversion pathways at widely separated points via salvage pathways (galactokinase and hexokinase, respectively), which permits an evaluation of the major routes toward the synthesis of specific nucleotide sugars. The overall conclusion of this study is that UDP-GlcA is primarily synthesized via oxidation of UDP-Glc to UDP-GlcA, UDP-GalA is primarily synthesized via 4-epimerization of UDP-GlcA, and GDP-Glc is primarily synthesized by guanylyl transfer from GTP onto glucose-1-phosphate.
    • (2007) Plant J , vol.52 , pp. 252-262
    • Sharples, S.C.1    Fry, S.C.2
  • 18
    • 3543019727 scopus 로고    scopus 로고
    • The biosynthesis of d-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-d-glucuronate 4-epimerase from Arabidopsis
    • Mølhøj M., Verma R., and Reiter W.-D. The biosynthesis of d-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-d-glucuronate 4-epimerase from Arabidopsis. Plant Physiol 135 (2004) 1221-1230
    • (2004) Plant Physiol , vol.135 , pp. 1221-1230
    • Mølhøj, M.1    Verma, R.2    Reiter, W.-D.3
  • 19
    • 16644371952 scopus 로고    scopus 로고
    • The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-d-glucuronic acid 4-epimerase
    • Gu X., and Bar-Peled M. The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-d-glucuronic acid 4-epimerase. Plant Physiol 136 (2004) 4256-4264
    • (2004) Plant Physiol , vol.136 , pp. 4256-4264
    • Gu, X.1    Bar-Peled, M.2
  • 20
    • 27944457216 scopus 로고    scopus 로고
    • Characterization of GDP-mannose pyrophosphorylase from Escherichia coli O157:H7 EDL933 and its broad substrate specificity
    • Yang Y.-H., Kang Y.-B., Lee K.-W., Lee T.-H., Park S.-S., Hwang B.-Y., and Kima B.-G. Characterization of GDP-mannose pyrophosphorylase from Escherichia coli O157:H7 EDL933 and its broad substrate specificity. J Mol Catal B: Enzymatic 37 (2005) 1-8
    • (2005) J Mol Catal B: Enzymatic , vol.37 , pp. 1-8
    • Yang, Y.-H.1    Kang, Y.-B.2    Lee, K.-W.3    Lee, T.-H.4    Park, S.-S.5    Hwang, B.-Y.6    Kima, B.-G.7
  • 21
    • 0014278985 scopus 로고
    • The purification and properties of guanosine diphosphate glucose pyrophosphorylase of pea seedlings
    • Péaud-Lenoël C., and Axelos M. The purification and properties of guanosine diphosphate glucose pyrophosphorylase of pea seedlings. Eur J Biochem 4 (1968) 561-567
    • (1968) Eur J Biochem , vol.4 , pp. 561-567
    • Péaud-Lenoël, C.1    Axelos, M.2
  • 23
    • 0035956885 scopus 로고    scopus 로고
    • Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate guanylyltransferase and point to a requirement of N-linked glycosylation for cellulose biosynthesis
    • Lukowitz W., Nickle T.C., Meinke D.W., Last R.L., Conklin P.L., and Somerville C.R. Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate guanylyltransferase and point to a requirement of N-linked glycosylation for cellulose biosynthesis. Proc Natl Acad Sci U S A 98 (2001) 2262-2267
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2262-2267
    • Lukowitz, W.1    Nickle, T.C.2    Meinke, D.W.3    Last, R.L.4    Conklin, P.L.5    Somerville, C.R.6
  • 24
    • 17644402491 scopus 로고    scopus 로고
    • Biosynthesis of UDP-GlcA: via UDPGDH or myo-inositol oxidation pathway?
    • Kärkönen A. Biosynthesis of UDP-GlcA: via UDPGDH or myo-inositol oxidation pathway?. Plant Biosyst 139 (2005) 46-49
    • (2005) Plant Biosyst , vol.139 , pp. 46-49
    • Kärkönen, A.1
  • 25
    • 1642506227 scopus 로고    scopus 로고
    • Myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis
    • Lorence A., Chevone B.I., Mendes P., and Nessler C.L. Myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis. Plant Physiol 134 (2004) 1200-1205
    • (2004) Plant Physiol , vol.134 , pp. 1200-1205
    • Lorence, A.1    Chevone, B.I.2    Mendes, P.3    Nessler, C.L.4
  • 26
    • 18644381680 scopus 로고    scopus 로고
    • The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides
    • Kanter U., Usadel B., Guerineau F., Li Y., Pauly M., and Tenhaken R. The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides. Planta 221 (2005) 243-254
    • (2005) Planta , vol.221 , pp. 243-254
    • Kanter, U.1    Usadel, B.2    Guerineau, F.3    Li, Y.4    Pauly, M.5    Tenhaken, R.6
  • 27
    • 37649009222 scopus 로고    scopus 로고
    • Phloem loading in Verbascum phoeniceum L. depends on the synthesis of raffinose-family oligosaccharides
    • McCaskill A., and Turgeon R. Phloem loading in Verbascum phoeniceum L. depends on the synthesis of raffinose-family oligosaccharides. Proc Natl Acad Sci U S A 104 (2007) 19619-19624
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19619-19624
    • McCaskill, A.1    Turgeon, R.2
  • 28
    • 0030296227 scopus 로고    scopus 로고
    • Cloning of an enzyme that synthesizes a key nucleotide sugar precursor of hemicellulose biosynthesis from soybean: UDP-glucose dehydrogenase
    • Tenhaken R., and Thulke O. Cloning of an enzyme that synthesizes a key nucleotide sugar precursor of hemicellulose biosynthesis from soybean: UDP-glucose dehydrogenase. Plant Physiol 112 (1996) 1127-1134
    • (1996) Plant Physiol , vol.112 , pp. 1127-1134
    • Tenhaken, R.1    Thulke, O.2
  • 29
    • 33745261717 scopus 로고    scopus 로고
    • Reconstruction of de novo pathway for synthesis of UDP-glucuronic acid and UDP-xylose from intrinsic UDP-glucose in Saccharomyces cerevisiae
    • i value of about 5 μM.
    • i value of about 5 μM. These results suggest that feedback inhibition of plant nucleotide sugar interconversion enzymes is sufficient to stabilize the pool size of nucleotide sugars even if the reactions are highly exergonic and the end products are not further metabolized.
    • (2006) FEBS J , vol.273 , pp. 2645-2657
    • Oka, T.1    Jigami, Y.2
  • 33
    • 0017865516 scopus 로고
    • The formation of UDP-l-rhamnose from UDP-d-glucose by an enzyme preparation of red campion (Silene dioica (L) Clairv) leaves
    • Kamsteeg J., Van Brederode J., and Van Nigtevecht G. The formation of UDP-l-rhamnose from UDP-d-glucose by an enzyme preparation of red campion (Silene dioica (L) Clairv) leaves. FEBS Lett 91 (1978) 281-284
    • (1978) FEBS Lett , vol.91 , pp. 281-284
    • Kamsteeg, J.1    Van Brederode, J.2    Van Nigtevecht, G.3
  • 34
    • 34247099779 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-d-glucose to UDP-l-rhamnose conversion
    • The three predicted isoforms of UDP-Rha synthase from Arabidopsis (RHM1, RHM2 and RHM3) were heterologously expressed in S. cerevisiae and shown to have the expected enzymatic activity in vitro. This biochemical study focuses on isoform RHM2, which contains missense mutations in both alleles of the mucilage modified4 (mum4) mutants. The authors demonstrate that the N-terminal domain of RHM2 acts as a UDP-Glc 4,6-dehydratase, and that the C-terminal domain acts as a 3,5-epimerase-4-reductase that converts the reaction intermediate into UDP-Rha. Enzyme assays on RHM2 variants that contain the amino substitutions in MUM4-1 and MUM4-2 did not reveal any activity. This provides biochemical evidence that the seed coat mucilage phenotype of mum4 plants is caused by defects in a rhamnose-biosynthetic gene.
    • Oka T., Nemoto T., and Jigami Y. Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-d-glucose to UDP-l-rhamnose conversion. J Biol Chem 282 (2007) 5389-5403. The three predicted isoforms of UDP-Rha synthase from Arabidopsis (RHM1, RHM2 and RHM3) were heterologously expressed in S. cerevisiae and shown to have the expected enzymatic activity in vitro. This biochemical study focuses on isoform RHM2, which contains missense mutations in both alleles of the mucilage modified4 (mum4) mutants. The authors demonstrate that the N-terminal domain of RHM2 acts as a UDP-Glc 4,6-dehydratase, and that the C-terminal domain acts as a 3,5-epimerase-4-reductase that converts the reaction intermediate into UDP-Rha. Enzyme assays on RHM2 variants that contain the amino substitutions in MUM4-1 and MUM4-2 did not reveal any activity. This provides biochemical evidence that the seed coat mucilage phenotype of mum4 plants is caused by defects in a rhamnose-biosynthetic gene.
    • (2007) J Biol Chem , vol.282 , pp. 5389-5403
    • Oka, T.1    Nemoto, T.2    Jigami, Y.3
  • 35
    • 0842328849 scopus 로고    scopus 로고
    • RHM2 is involved in mucilage pectin biosynthesis and is required for the development of the seed coat in Arabidopsis
    • Usadel B., Kuschinsky A.M., Rosso M.G., Eckermann N., and Pauly M. RHM2 is involved in mucilage pectin biosynthesis and is required for the development of the seed coat in Arabidopsis. Plant Physiol 134 (2004) 286-295
    • (2004) Plant Physiol , vol.134 , pp. 286-295
    • Usadel, B.1    Kuschinsky, A.M.2    Rosso, M.G.3    Eckermann, N.4    Pauly, M.5
  • 36
    • 0842285681 scopus 로고    scopus 로고
    • MUCILAGE-MODIFIED4 encodes a putative pectin biosynthetic enzyme developmentally regulated by APETALA2, TRANSPARENT TESTA GLABRA1, and GLABRA2 in the Arabidopsis seed coat
    • Western T.L., Young D.S., Dean G.H., Tan W.L., Samuels A.L., and Haughn G.W. MUCILAGE-MODIFIED4 encodes a putative pectin biosynthetic enzyme developmentally regulated by APETALA2, TRANSPARENT TESTA GLABRA1, and GLABRA2 in the Arabidopsis seed coat. Plant Physiol 134 (2004) 296-306
    • (2004) Plant Physiol , vol.134 , pp. 296-306
    • Western, T.L.1    Young, D.S.2    Dean, G.H.3    Tan, W.L.4    Samuels, A.L.5    Haughn, G.W.6
  • 37
    • 1942501864 scopus 로고    scopus 로고
    • A bifunctional 3,5-epimerase/4-keto reductase for nucleotide-rhamnose synthesis in Arabidopsis
    • Watt G., Leoff C., Harper A.D., and Bar-Peled M. A bifunctional 3,5-epimerase/4-keto reductase for nucleotide-rhamnose synthesis in Arabidopsis. Plant Physiol 134 (2004) 1337-1346
    • (2004) Plant Physiol , vol.134 , pp. 1337-1346
    • Watt, G.1    Leoff, C.2    Harper, A.D.3    Bar-Peled, M.4
  • 38
    • 33745780270 scopus 로고    scopus 로고
    • The Arabidopsis root hair cell wall formation mutant lrx1 is suppressed by mutations in the RHM1 gene encoding a UDP-l-rhamnose synthase
    • A mutant screen was conducted to identify suppressors of the abnormal root hair morphology found in Arabidopsis plants that carry mutations in the cell wall protein LRX1. This protein consists of a leucine-rich repeat fused to a domain that resembles hydroxyproline-rich glycoproteins (HRGPs, also referred to as extensins). The suppressor locus rol1 (repressor of lrx1) turned out to have mutations in isoform RHM1 of UDP-Rha synthase that abolish enzymatic activity in vitro. Although the rol1 mutations were found to cause changes in rhamnogalacturonans I and II, the molecular mechanism underlying the suppressor phenotype remains to be determined.
    • Diet A., Link B., Seifert G.J., Schellenberg B., Wagner U., Pauly M., Reiter W.-D., and Ringli C. The Arabidopsis root hair cell wall formation mutant lrx1 is suppressed by mutations in the RHM1 gene encoding a UDP-l-rhamnose synthase. Plant Cell 18 (2006) 1630-1641. A mutant screen was conducted to identify suppressors of the abnormal root hair morphology found in Arabidopsis plants that carry mutations in the cell wall protein LRX1. This protein consists of a leucine-rich repeat fused to a domain that resembles hydroxyproline-rich glycoproteins (HRGPs, also referred to as extensins). The suppressor locus rol1 (repressor of lrx1) turned out to have mutations in isoform RHM1 of UDP-Rha synthase that abolish enzymatic activity in vitro. Although the rol1 mutations were found to cause changes in rhamnogalacturonans I and II, the molecular mechanism underlying the suppressor phenotype remains to be determined.
    • (2006) Plant Cell , vol.18 , pp. 1630-1641
    • Diet, A.1    Link, B.2    Seifert, G.J.3    Schellenberg, B.4    Wagner, U.5    Pauly, M.6    Reiter, W.-D.7    Ringli, C.8
  • 39
    • 17644409786 scopus 로고    scopus 로고
    • The role of extracellular LRR-extensin (LRX) proteins in cell wall formation
    • Ringli C. The role of extracellular LRR-extensin (LRX) proteins in cell wall formation. Plant Biosyst 139 (2005) 32-35
    • (2005) Plant Biosyst , vol.139 , pp. 32-35
    • Ringli, C.1
  • 40
    • 0035337065 scopus 로고    scopus 로고
    • The chimeric leucine-rich repeat/extensin cell wall protein LRX1 is required for root hair morphogenesis in Arabidopsis thaliana
    • Baumberger N., Ringli C., and Keller B. The chimeric leucine-rich repeat/extensin cell wall protein LRX1 is required for root hair morphogenesis in Arabidopsis thaliana. Genes Dev 15 (2001) 1128-1139
    • (2001) Genes Dev , vol.15 , pp. 1128-1139
    • Baumberger, N.1    Ringli, C.2    Keller, B.3
  • 41
    • 4544322505 scopus 로고    scopus 로고
    • The composition and structure of plant primary cell walls
    • Rose J.K.C. (Ed), Blackwell, Oxford
    • O'Neill M.A., and York W.S. The composition and structure of plant primary cell walls. In: Rose J.K.C. (Ed). The Plant Cell Wall (2003), Blackwell, Oxford 1-54
    • (2003) The Plant Cell Wall , pp. 1-54
    • O'Neill, M.A.1    York, W.S.2
  • 42
    • 0037329646 scopus 로고    scopus 로고
    • The biosynthesis of l-arabinose in plants: molecular cloning and characterization of a Golgi-localized UDP-d-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis
    • Burget E.G., Verma R., Mølhøj M., and Reiter W.D. The biosynthesis of l-arabinose in plants: molecular cloning and characterization of a Golgi-localized UDP-d-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis. Plant Cell 15 (2003) 523-531
    • (2003) Plant Cell , vol.15 , pp. 523-531
    • Burget, E.G.1    Verma, R.2    Mølhøj, M.3    Reiter, W.D.4
  • 43
    • 0000846948 scopus 로고
    • Sugar-nucleotide precursors of arabinopyranosyl, arabinofuranosyl, and xylopyranosyl residues in spinach polysaccharides
    • Fry S.C., and Northcote D.H. Sugar-nucleotide precursors of arabinopyranosyl, arabinofuranosyl, and xylopyranosyl residues in spinach polysaccharides. Plant Physiol 73 (1983) 1055-1061
    • (1983) Plant Physiol , vol.73 , pp. 1055-1061
    • Fry, S.C.1    Northcote, D.H.2
  • 44
    • 33745963005 scopus 로고    scopus 로고
    • Identification of a mung bean arabinofuranosyltransferase that transfers arabinofuranosyl residues onto (1,5)-linked α-l-arabino-oligosaccharides
    • Konishi T., Ono H., Ohnishi-Kameyama M., Kaneko S., and Ishii T. Identification of a mung bean arabinofuranosyltransferase that transfers arabinofuranosyl residues onto (1,5)-linked α-l-arabino-oligosaccharides. Plant Physiol 141 (2006) 1098-1105
    • (2006) Plant Physiol , vol.141 , pp. 1098-1105
    • Konishi, T.1    Ono, H.2    Ohnishi-Kameyama, M.3    Kaneko, S.4    Ishii, T.5
  • 46
    • 0035931587 scopus 로고    scopus 로고
    • Chemical synthesis of UDP-β-l-arabinofuranose and its turnover to UDP-β-l-arabinopyranose by UDP-galactopyranose mutase
    • Zhang Q., and Liu H.-W. Chemical synthesis of UDP-β-l-arabinofuranose and its turnover to UDP-β-l-arabinopyranose by UDP-galactopyranose mutase. Bioorg Med Chem Lett 11 (2001) 145-149
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 145-149
    • Zhang, Q.1    Liu, H.-W.2
  • 47
    • 33847345130 scopus 로고    scopus 로고
    • A plant mutase that interconverts UDP-arabinofuranose and UDP-arabinopyranose
    • Arabinose residues in plant cell wall material exist predominantly in their furanose form although this configuration is thermodynamically less stable than the pyranose form generated by the 4-epimerization of UDP-d-xylopyranose. This raises the question whether most arabinosyltransferases can catalyze the necessary ring contraction, or whether an unknown mutase catalyzes an interconversion between UDP-l-Arap and UDP-l-Araf. The authors addressed this issue by purifying UDP-l-Arap mutase activity from rice seedlings and cloning the corresponding gene. The mutase activity turned out to be a property of reversibly glycosylated proteins (RGPs) for which the biological function had not previously been established.
    • Konishi T., Takeda T., Miyazaki Y., Ohnishi-Kameyama M., Hayashi T., O'Neill M.A., and Ishii T. A plant mutase that interconverts UDP-arabinofuranose and UDP-arabinopyranose. Glycobiology 17 (2007) 345-354. Arabinose residues in plant cell wall material exist predominantly in their furanose form although this configuration is thermodynamically less stable than the pyranose form generated by the 4-epimerization of UDP-d-xylopyranose. This raises the question whether most arabinosyltransferases can catalyze the necessary ring contraction, or whether an unknown mutase catalyzes an interconversion between UDP-l-Arap and UDP-l-Araf. The authors addressed this issue by purifying UDP-l-Arap mutase activity from rice seedlings and cloning the corresponding gene. The mutase activity turned out to be a property of reversibly glycosylated proteins (RGPs) for which the biological function had not previously been established.
    • (2007) Glycobiology , vol.17 , pp. 345-354
    • Konishi, T.1    Takeda, T.2    Miyazaki, Y.3    Ohnishi-Kameyama, M.4    Hayashi, T.5    O'Neill, M.A.6    Ishii, T.7
  • 48
    • 0025721904 scopus 로고
    • Plant polypeptides reversibly glycosylated by UDP-glucose - possible components of Golgi β-glucan synthase in pea cells
    • Dhugga K.S., Ulvskov P., Gallagher S.R., and Ray P.M. Plant polypeptides reversibly glycosylated by UDP-glucose - possible components of Golgi β-glucan synthase in pea cells. J Biol Chem 266 (1991) 21977-21984
    • (1991) J Biol Chem , vol.266 , pp. 21977-21984
    • Dhugga, K.S.1    Ulvskov, P.2    Gallagher, S.R.3    Ray, P.M.4
  • 49
    • 0032036352 scopus 로고    scopus 로고
    • Cloning and characterization of AtRGP1-a reversibly autoglycosylated Arabidopsis protein implicated in cell wall biosynthesis
    • Delgado I.J., Wang Z., de Rocher A., Keegstra K., and Raikhel N. Cloning and characterization of AtRGP1-a reversibly autoglycosylated Arabidopsis protein implicated in cell wall biosynthesis. Plant Physiol 116 (1998) 1339-1349
    • (1998) Plant Physiol , vol.116 , pp. 1339-1349
    • Delgado, I.J.1    Wang, Z.2    de Rocher, A.3    Keegstra, K.4    Raikhel, N.5
  • 50
    • 0030737904 scopus 로고    scopus 로고
    • A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: purification, gene cloning, and trans-Golgi localization
    • Dhugga K.S., Tiwari S.C., and Ray P.M. A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: purification, gene cloning, and trans-Golgi localization. Proc Natl Acad Sci U S A 94 (1997) 7679-7684
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7679-7684
    • Dhugga, K.S.1    Tiwari, S.C.2    Ray, P.M.3
  • 51
    • 33845645054 scopus 로고    scopus 로고
    • Arabidopsis reversibly glycosylated polypeptides 1 and 2 are essential for pollen development
    • Drakakaki G., Zabotina O., Delgado I., Robert S., Keegstra K., and Raikhel N. Arabidopsis reversibly glycosylated polypeptides 1 and 2 are essential for pollen development. Plant Physiol 142 (2006) 1480-1492
    • (2006) Plant Physiol , vol.142 , pp. 1480-1492
    • Drakakaki, G.1    Zabotina, O.2    Delgado, I.3    Robert, S.4    Keegstra, K.5    Raikhel, N.6
  • 52
    • 35348830463 scopus 로고    scopus 로고
    • Signaling from an altered cell wall to the nucleus mediates sugar-responsive growth and development in Arabidopsis thaliana
    • Li Y., Smith C., Corke F., Zheng L., Merali Z., Ryden P., Derbyshire P., Waldron K., and Bevan M.W. Signaling from an altered cell wall to the nucleus mediates sugar-responsive growth and development in Arabidopsis thaliana. Plant Cell 19 (2007) 2500-2515
    • (2007) Plant Cell , vol.19 , pp. 2500-2515
    • Li, Y.1    Smith, C.2    Corke, F.3    Zheng, L.4    Merali, Z.5    Ryden, P.6    Derbyshire, P.7    Waldron, K.8    Bevan, M.W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.