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1
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0001060734
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Biosynthesis of pectins and galactomannans
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Edited by Barton SD, Nakanisho H, Meth-Cohn O, Pinto BM. Amsterdam: Elsevier Publishing;
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Mohnen D: Biosynthesis of pectins and galactomannans. In Carbohydrates and Their Derivatives Including Tannins, Cellulose, and Related Lignins. Edited by Barton SD, Nakanisho H, Meth-Cohn O, Pinto BM. Amsterdam: Elsevier Publishing; 1999:498-527.
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Carbohydrates and Their Derivatives Including Tannins, Cellulose, and Related Lignins
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Mohnen, D.1
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2
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0346306092
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Why are there so many carbohydrate-active enzyme-related genes in plants?
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Coutinho P.M., Stam M., Blanc E., Henrissat B. Why are there so many carbohydrate-active enzyme-related genes in plants? Trends Plant Sci. 8:2003;563-565
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Trends Plant Sci
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Coutinho, P.M.1
Stam, M.2
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Henrissat, B.4
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4
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An evolving hierarchical family classification for glycosyltransferases
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Coutinho P.M., Deleury E., Davies G.J., Henrissat B. An evolving hierarchical family classification for glycosyltransferases. J Mol Biol. 328:2003;307-317
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J Mol Biol
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Coutinho, P.M.1
Deleury, E.2
Davies, G.J.3
Henrissat, B.4
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5
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0037020174
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In vitro versus in vivo cellulose microfibrils from plant primary wall synthases: Structural differences
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This is the first paper to report the production of significant amounts of plant cellulose in an in vitro system. Microsomal fractions that were extracted from suspension-cultured cells of blackberry using taurocholate or Brij58 detergents were able to synthesize substantial percentages (∼20%) of cellulose microfibrils together with callose. The cellulose formed in vitro was compared to cellulose produced in vivo using a range of analyses, such as resistance to the Updegraff reagent, methylation analysis, electron microscopy, and electron and X-ray synchroton diffractions. The structures of the in vivo and in vitro products were similar, but the in vitro product had higher perfection and crystallinity as well as better resistance to the Updegraff reagent.
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Lai-Kee-Him J., Chanzy H., Müller M., Puteaux J-L., Imai T., Bulone V. In vitro versus in vivo cellulose microfibrils from plant primary wall synthases: structural differences. J Biol Chem. 277:2002;36931-36939 This is the first paper to report the production of significant amounts of plant cellulose in an in vitro system. Microsomal fractions that were extracted from suspension-cultured cells of blackberry using taurocholate or Brij58 detergents were able to synthesize substantial percentages (∼20%) of cellulose microfibrils together with callose. The cellulose formed in vitro was compared to cellulose produced in vivo using a range of analyses, such as resistance to the Updegraff reagent, methylation analysis, electron microscopy, and electron and X-ray synchroton diffractions. The structures of the in vivo and in vitro products were similar, but the in vitro product had higher perfection and crystallinity as well as better resistance to the Updegraff reagent.
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J Biol Chem
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Lai-Kee-Him, J.1
Chanzy, H.2
Müller, M.3
Puteaux, J.-L.4
Imai, T.5
Bulone, V.6
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6
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0036883487
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Biosynthesis and properties of the plant cell wall
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Reiter W-D. Biosynthesis and properties of the plant cell wall. Curr Opin Plant Biol. 5:2002;536-542
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Curr Opin Plant Biol
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Reiter, W.-D.1
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7
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0034486470
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Multiple cellulose synthase catalytic subunits are required for cellulose synthesis in Arabidopsis
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Taylor N.G., Laurie S., Turner S.R. Multiple cellulose synthase catalytic subunits are required for cellulose synthesis in Arabidopsis. Plant Cell. 12:2000;2529-2540
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Plant Cell
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Taylor, N.G.1
Laurie, S.2
Turner, S.R.3
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8
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0035964260
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Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants
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Scheible W-R., Eshed R., Richmond T., Delmer D., Somerville C. Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants. Proc Natl Acad Sci USA. 98:2001;10079-10084
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Proc Natl Acad Sci USA
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Scheible, W.-R.1
Eshed, R.2
Richmond, T.3
Delmer, D.4
Somerville, C.5
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9
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0035916821
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Cellulose: How many cellulose synthases to make a plant?
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Perrin R.M. Cellulose: how many cellulose synthases to make a plant? Curr Biol. 11:2001;R213-R216
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Curr Biol
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Perrin, R.M.1
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11
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0037417818
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Interactions among three distinct CESA proteins essential for cellulose synthesis
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The authors identify a novel irregular xylem complementation group (irx5), and show that the affected gene encodes AtCESA4. irx5 plants have a phenotype that is identical to that of previously described mutants that have defects in two other members of the CESA gene family (IRX1 and IRX3). The three CESA isoforms are co-expressed in exactly the same cells, and interact in detergent-solubilized extracts. These findings suggest that IRX5, IRX3 and IRX1 are all essential components of the secondary cellulose-synthase complex.
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Taylor N.G., Howells R.M., Huttly A.K., Vickers K., Turner S.R. Interactions among three distinct CESA proteins essential for cellulose synthesis. Proc Natl Acad Sci USA. 100:2003;1450-1455 The authors identify a novel irregular xylem complementation group (irx5), and show that the affected gene encodes AtCESA4. irx5 plants have a phenotype that is identical to that of previously described mutants that have defects in two other members of the CESA gene family (IRX1 and IRX3). The three CESA isoforms are co-expressed in exactly the same cells, and interact in detergent-solubilized extracts. These findings suggest that IRX5, IRX3 and IRX1 are all essential components of the secondary cellulose-synthase complex.
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(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 1450-1455
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Taylor, N.G.1
Howells, R.M.2
Huttly, A.K.3
Vickers, K.4
Turner, S.R.5
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12
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0141787882
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Three distinct rice cellulose synthase catalytic subunit genes required for cellulose synthesis in the secondary wall
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Tanaka K., Murata K., Yamazaki M., Onosato K., Miyao A., Hirochika H. Three distinct rice cellulose synthase catalytic subunit genes required for cellulose synthesis in the secondary wall. Plant Physiol. 133:2003;73-83
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(2003)
Plant Physiol
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, pp. 73-83
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Tanaka, K.1
Murata, K.2
Yamazaki, M.3
Onosato, K.4
Miyao, A.5
Hirochika, H.6
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13
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2442606473
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Plant cell wall synthesis: Making the bricks
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Edited by Rose JCK. Sheffield: Blackwell Publishing - CRC Press;
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Doblin MS, Vergara CE, Read S, Newbigin E, Bacic A: Plant cell wall synthesis: making the bricks. In Annual Plant Reviews, vol 8. The Plant Cell Wall. Edited by Rose JCK. Sheffield: Blackwell Publishing - CRC Press; 2003:183-222.
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(2003)
Annual Plant Reviews, Vol 8. the Plant Cell Wall
, vol.8
, pp. 183-222
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Doblin, M.S.1
Vergara, C.E.2
Read, S.3
Newbigin, E.4
Bacic, A.5
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14
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0035983662
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Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis
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Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E. Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis. Plant Physiol. 129:2002;797-807
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Plant Physiol
, vol.129
, pp. 797-807
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Burn, J.E.1
Hocart, C.H.2
Birch, R.J.3
Cork, A.C.4
Williamson, R.E.5
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15
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0346037064
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Genetic complexity of cellulose synthase a gene function in Arabidopsis embryogenesis
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The authors report that only four of ten CESA genes, CESA1, CESA2, CESA3 and CESA9, are significantly expressed in the Arabidopsis embryo. They identify a null mutation in the RADIALLY SWOLLEN1 (RSW1/CESA1) gene of Arabidopsis that by the time of embryogenesis, already interferes with cell division and expansion. Primary cell walls are still formed during embryogenesis in the rsw1 mutant but are thin, highly undulated and frequently interrupted. From the heart-stage onward, cell elongation in the embryo axis of rsw1 is severely impaired, and cell width is disproportionately increased. CESA1, CESA2, CESA3, and CESA9 are expressed in largely overlapping domains within the embryo and may act cooperatively in higher-order complexes. The embryonic phenotype of the presumed rsw1 null mutant indicates that the RSW1 (CESA1) product has a crucial nonredundant function, but is not strictly required for primary cell wall formation.
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Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R., Inzé D., Berleth T. Genetic complexity of cellulose synthase A gene function in Arabidopsis embryogenesis. Plant Physiol. 130:2002;1883-1893 The authors report that only four of ten CESA genes, CESA1, CESA2, CESA3 and CESA9, are significantly expressed in the Arabidopsis embryo. They identify a null mutation in the RADIALLY SWOLLEN1 (RSW1/CESA1) gene of Arabidopsis that by the time of embryogenesis, already interferes with cell division and expansion. Primary cell walls are still formed during embryogenesis in the rsw1 mutant but are thin, highly undulated and frequently interrupted. From the heart-stage onward, cell elongation in the embryo axis of rsw1 is severely impaired, and cell width is disproportionately increased. CESA1, CESA2, CESA3, and CESA9 are expressed in largely overlapping domains within the embryo and may act cooperatively in higher-order complexes. The embryonic phenotype of the presumed rsw1 null mutant indicates that the RSW1 (CESA1) product has a crucial nonredundant function, but is not strictly required for primary cell wall formation.
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(2002)
Plant Physiol
, vol.130
, pp. 1883-1893
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Beeckman, T.1
Przemeck, G.K.H.2
Stamatiou, G.3
Lau, R.4
Terryn, N.5
De Rycke, R.6
Inzé, D.7
Berleth, T.8
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16
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0037143690
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Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains
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This study provides evidence that the dimerization of the catalytic subunits of cellulose synthase is subject to redox modulation. Oxidative conditions should favor the formation of cellulose synthase complexes and cellulose synthesis, whereas CESA monomers might be subject to RING-finger-mediated protein degradation under reductive conditions.
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Kurek I., Kawagoe Y., Jacob-Wilk D., Doblin M., Delmer D. Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains. Proc Natl Acad Sci USA. 99:2002;11109-11114 This study provides evidence that the dimerization of the catalytic subunits of cellulose synthase is subject to redox modulation. Oxidative conditions should favor the formation of cellulose synthase complexes and cellulose synthesis, whereas CESA monomers might be subject to RING-finger-mediated protein degradation under reductive conditions.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 11109-11114
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Kurek, I.1
Kawagoe, Y.2
Jacob-Wilk, D.3
Doblin, M.4
Delmer, D.5
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17
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0032770495
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The involvement of hydrogen peroxide in the differentiation of secondary walls in cotton fibers
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Potikha T.S., Collins C.C., Johnson D.I., Delmer D.P., Levine A. The involvement of hydrogen peroxide in the differentiation of secondary walls in cotton fibers. Plant Physiol. 119:1999;849-858
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(1999)
Plant Physiol
, vol.119
, pp. 849-858
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Potikha, T.S.1
Collins, C.C.2
Johnson, D.I.3
Delmer, D.P.4
Levine, A.5
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18
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0036743460
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Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: A novel regulatory mechanism linking starch synthesis to the sucrose supply
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The work described in this manuscript provides evidence that the key enzyme in starch synthesis, AGPase, is regulated by redox modulation. Starch synthesis is inhibited in detached potato tubers: although overall AGPase activity remains high, the substrates ATP and glucose-1-P increase, and the 3-phosphoglycerate (3-PGA)/inorganic phosphate (Pi) ratio increases. This inhibition of starch synthesis does not occur in transgenic tubers that express a heterologous AGPase, and changes in the subcellular levels of AGPase substrates reveal that AGPase itself is involved in the inhibition. The authors demonstrate that the inhibition of starch synthesis is due to oxidative dimerization, and thus to the deactivation of the AGPase catalytic subunit (AGPB) as a result of its reduced substrate affinity and sensitivity to allosteric effectors. The dimerization can be reversed and AGPase reactivated in vitro by incubating extracts with dithiothreitol (DTT)
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Tiessen A., Hendriks J.H., Stitt M., Branscheid A., Gibon Y., Farre E.M., Geigenberger P. Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply. Plant Cell. 14:2002;2191-2213 The work described in this manuscript provides evidence that the key enzyme in starch synthesis, AGPase, is regulated by redox modulation. Starch synthesis is inhibited in detached potato tubers: although overall AGPase activity remains high, the substrates ATP and glucose-1-P increase, and the 3-phosphoglycerate (3-PGA)/inorganic phosphate (Pi) ratio increases. This inhibition of starch synthesis does not occur in transgenic tubers that express a heterologous AGPase, and changes in the subcellular levels of AGPase substrates reveal that AGPase itself is involved in the inhibition. The authors demonstrate that the inhibition of starch synthesis is due to oxidative dimerization, and thus to the deactivation of the AGPase catalytic subunit (AGPB) as a result of its reduced substrate affinity and sensitivity to allosteric effectors. The dimerization can be reversed and AGPase reactivated in vitro by incubating extracts with dithiothreitol (DTT). The incubation of tuber slices with DTT or in concentrations of high sucrose reduces dimerization, increases AGPase activation, and stimulates starch synthesis in vivo.
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(2002)
Plant Cell
, vol.14
, pp. 2191-2213
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Tiessen, A.1
Hendriks, J.H.2
Stitt, M.3
Branscheid, A.4
Gibon, Y.5
Farre, E.M.6
Geigenberger, P.7
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19
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0142214642
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ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species
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•], the authors show that AGPase is also subject to posttranslational redox regulation in the leaves of pea, potato and Arabidopsis. Light and sugars act as inputs to trigger the posttranslational regulation of AGPase.
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•], the authors show that AGPase is also subject to posttranslational redox regulation in the leaves of pea, potato and Arabidopsis. Light and sugars act as inputs to trigger the posttranslational regulation of AGPase.
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(2003)
Plant Physiol
, vol.133
, pp. 838-849
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Hendriks, J.H.1
Kolbe, A.2
Gibon, Y.3
Stitt, M.4
Geigenberger, P.5
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20
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0036741541
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KOBITO1 encodes a novel plasma membrane protein necessary for normal synthesis of cellulose during cell expansion in Arabidopsis
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The authors identified the kob1 T-DNA insertion mutant of Arabidopsis in a screen for mutants that show reduced growth anisotrophy in dark-grown hypocotyls. The affected gene encodes a novel plant-specific plasma-membrane-localized protein. kob1 plants show incomplete cell walls in hypocotyls cells, slightly increased pectin content, unaltered xyloglucan structure, accumulation of ectopic lignin and callose, and a 30-40% reduction in cellulose content. In contrast to wildtype plants, which have transversely oriented parallel microfibrils, kob1 plants have microfibrils that are randomized in rapidly elongating cells. The authors suggest that KOB1 either is part of the cellulose synthesis machinery in elongating cells or could play a role in coordinating cell elongation and cellulose synthesis.
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Pagant S., Bichet A., Sugimoto K., Lerouxel O., Desprez T., McCann M., Lerouge P., Vernhettes S., Höfte H. KOBITO1 encodes a novel plasma membrane protein necessary for normal synthesis of cellulose during cell expansion in Arabidopsis. Plant Cell. 14:2002;2001-2013 The authors identified the kob1 T-DNA insertion mutant of Arabidopsis in a screen for mutants that show reduced growth anisotrophy in dark-grown hypocotyls. The affected gene encodes a novel plant-specific plasma-membrane-localized protein. kob1 plants show incomplete cell walls in hypocotyls cells, slightly increased pectin content, unaltered xyloglucan structure, accumulation of ectopic lignin and callose, and a 30-40% reduction in cellulose content. In contrast to wildtype plants, which have transversely oriented parallel microfibrils, kob1 plants have microfibrils that are randomized in rapidly elongating cells. The authors suggest that KOB1 either is part of the cellulose synthesis machinery in elongating cells or could play a role in coordinating cell elongation and cellulose synthesis.
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(2002)
Plant Cell
, vol.14
, pp. 2001-2013
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Pagant, S.1
Bichet, A.2
Sugimoto, K.3
Lerouxel, O.4
Desprez, T.5
McCann, M.6
Lerouge, P.7
Vernhettes, S.8
Höfte, H.9
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21
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A mutant of Arabidopsis thaliana displaying altered patterns of cellulose deposition
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Potikha T., Delmer D.P. A mutant of Arabidopsis thaliana displaying altered patterns of cellulose deposition. Plant J. 7:1995;453-460
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Plant J
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Potikha, T.1
Delmer, D.P.2
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0028847509
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Mechanism of cellulose synthesis in Agrobacterium tumefaciens
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Matthysse A.G., Thomas D.O.L., White A.L. Mechanism of cellulose synthesis in Agrobacterium tumefaciens. J Bacteriol. 177:1995;1076-1081
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J Bacteriol
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Matthysse, A.G.1
Thomas, D.O.L.2
White, A.L.3
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23
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0037016399
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Sitosterol-beta-glucoside as primer for cellulose synthesis in plants
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Biochemical evidence shows that sitosterol-β-glucoside acts as a substrate for cotton CESA glucosyltransferase during sitosterol cellodextrin formation in vitro, and that sitosterol cellodextrin intermediates can be incorporated into high-molecular-weight products. This suggests that sitosterol-β-glucoside may act as a primer for cellulose synthesis. The cellulase encoded by the KOR gene, which is required for cellulose synthesis in plants, may function to cleave sitosterol-β-glucoside from the growing polymer chain.
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Peng L., Kawagoe Y., Hogan P., Delmer D. Sitosterol-beta-glucoside as primer for cellulose synthesis in plants. Science. 295:2002;147-150 Biochemical evidence shows that sitosterol-β-glucoside acts as a substrate for cotton CESA glucosyltransferase during sitosterol cellodextrin formation in vitro, and that sitosterol cellodextrin intermediates can be incorporated into high-molecular-weight products. This suggests that sitosterol-β-glucoside may act as a primer for cellulose synthesis. The cellulase encoded by the KOR gene, which is required for cellulose synthesis in plants, may function to cleave sitosterol-β-glucoside from the growing polymer chain.
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(2002)
Science
, vol.295
, pp. 147-150
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Peng, L.1
Kawagoe, Y.2
Hogan, P.3
Delmer, D.4
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24
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0037016493
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Plant biology. Prime time for cellulose
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Read S.M., Bacic T. Plant biology. Prime time for cellulose. Science. 295:2002;147-150
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(2002)
Science
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Read, S.M.1
Bacic, T.2
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25
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1942443154
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A link between sterol biosynthesis, the cell wall and cellulose in Arabidopsis
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••]. It is possible that sterols influence cell wall synthesis by yet unknown mechanisms.
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••]. It is possible that sterols influence cell wall synthesis by yet unknown mechanisms.
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Plant J
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Schrick, K.1
Fujioka, S.2
Takatsuto, S.3
Stierhof, Y.-D.4
Stransky, H.5
Yoshida, S.6
Jürgens, G.7
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26
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0033230547
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IFL1, a gene regulating interfascicular fiber differentiation in Arabidopsis, encodes a homeodomain-leucine zipper protein
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Zhong R., Ye Z.H. IFL1, a gene regulating interfascicular fiber differentiation in Arabidopsis, encodes a homeodomain-leucine zipper protein. Plant Cell. 11:1999;2139-2152
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Plant Cell
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Zhong, R.1
Ye, Z.H.2
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27
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0035143177
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REVOLUTA regulates meristem initiation at lateral positions
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Otsuga D., DeGuzman B., Prigge M.J., Drews G.N., Clark S.E. REVOLUTA regulates meristem initiation at lateral positions. Plant J. 25:2001;223-236
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Plant J
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, pp. 223-236
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Otsuga, D.1
Deguzman, B.2
Prigge, M.J.3
Drews, G.N.4
Clark, S.E.5
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28
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0034935422
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A putative plant homolog of the yeast beta-1,3-glucan synthase subunit FKS1 from cotton (Gossypium hirsutum L.) fibers
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Cui X., Shin H., Song C., Laosinchai W., Amano Y., Brown R.M. Jr. A putative plant homolog of the yeast beta-1, 3-glucan synthase subunit FKS1 from cotton (Gossypium hirsutum L.) fibers. Planta. 213:2001;223-230
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Planta
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Cui, X.1
Shin, H.2
Song, C.3
Laosinchai, W.4
Amano, Y.5
Brown Jr., R.M.6
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29
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0035032085
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A cell plate-specific callose synthase and its interaction with phragmoplastin
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Hong Z., Delauney A.J., Verma D.P. A cell plate-specific callose synthase and its interaction with phragmoplastin. Plant Cell. 13:2001;755-768
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Plant Cell
, vol.13
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Hong, Z.1
Delauney, A.J.2
Verma, D.P.3
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30
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0035027563
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Pollen tubes of Nicotiana alata express two genes from different beta-glucan synthase families
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Doblin M.S., De Melis L., Newbigin E., Bacic A., Read S.M. Pollen tubes of Nicotiana alata express two genes from different beta-glucan synthase families. Plant Physiol. 125:2001;2040-2052
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(2001)
Plant Physiol
, vol.125
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Doblin, M.S.1
De Melis, L.2
Newbigin, E.3
Bacic, A.4
Read, S.M.5
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31
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0041520958
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Loss of callose synthase results in salicylic acid-dependent disease resistance
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Arabidopsis pmr4 mutants have a lesion in a callose synthase gene and do not deposit callose in response to biotic or abiotic stress. Despite this lack of callose, the mutants are more resistant than wildtype plants to pathogen attack. Microarray experiments and double-mutant analyses reveal that this resistance is due to the activation of the salicylic acid defense signalling pathway. The authors conclude that callose or callose synthase negatively regulates the salicylic acid pathway.
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Nishimura M.T., Stein M., Hou B-H., Vogel J.P., Edwards H., Somerville S. Loss of callose synthase results in salicylic acid-dependent disease resistance. Science. 301:2003;969-972 Arabidopsis pmr4 mutants have a lesion in a callose synthase gene and do not deposit callose in response to biotic or abiotic stress. Despite this lack of callose, the mutants are more resistant than wildtype plants to pathogen attack. Microarray experiments and double-mutant analyses reveal that this resistance is due to the activation of the salicylic acid defense signalling pathway. The authors conclude that callose or callose synthase negatively regulates the salicylic acid pathway.
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(2003)
Science
, vol.301
, pp. 969-972
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Nishimura, M.T.1
Stein, M.2
Hou, B.-H.3
Vogel, J.P.4
Edwards, H.5
Somerville, S.6
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32
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0344514882
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An Arabidopsis callose synthase, GSL5, is required for wound and papillary callose formation
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••]).
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••]).
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(2003)
Plant Cell
, vol.15
, pp. 2503-2513
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Jacobs, A.K.1
Lipka, V.2
Burton, R.A.3
Panstruga, R.4
Strizhov, N.5
Schulze-Lefert, P.6
Fincher, G.B.7
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33
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0035984055
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The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses
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A mutant that has constitutively expressed stress-response genes is found to carry a mutation in the cellulose synthase catalytic subunit CESA3. The stress response in this mutant includes jasmonic acid and ethylene signalling and is caused by a reduction in cellulose synthesis. The same response occurs in wildtype plants that have been treated with inhibitors of cellulose synthesis.
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Ellis C., Karafyllidis I., Wasternack C., Turner J.G. The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses. Plant Cell. 14:2002;1557-1566 A mutant that has constitutively expressed stress-response genes is found to carry a mutation in the cellulose synthase catalytic subunit CESA3. The stress response in this mutant includes jasmonic acid and ethylene signalling and is caused by a reduction in cellulose synthesis. The same response occurs in wildtype plants that have been treated with inhibitors of cellulose synthesis.
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(2002)
Plant Cell
, vol.14
, pp. 1557-1566
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Ellis, C.1
Karafyllidis, I.2
Wasternack, C.3
Turner, J.G.4
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34
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0038367947
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Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana
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The authors show that the ectopic lignin mutations occur in the cellulose synthase gene CESA3 in Arabidopsis thaliana. These mutations cause reduced cellulose synthesis, and lead to constitutive stress responses and aberrant deposition of lignin by activating the ethylene and jasmonic acid signalling pathways. The results suggest that mechanisms that monitor cell wall integrity can activate lignification and defense responses.
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Caño-Delgado A., Penfield S., Smith C., Catley M., Bevan M. Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana. Plant J. 34:2003;351-362 The authors show that the ectopic lignin mutations occur in the cellulose synthase gene CESA3 in Arabidopsis thaliana. These mutations cause reduced cellulose synthesis, and lead to constitutive stress responses and aberrant deposition of lignin by activating the ethylene and jasmonic acid signalling pathways. The results suggest that mechanisms that monitor cell wall integrity can activate lignification and defense responses.
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Plant J
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Guar seed β-mannan synthase is a member of the cellulose synthase super gene family
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First evidence that a member of the CSL-gene family is involved in the synthesis of a wall polysaccharide other than cellulose. The authors cloned a cDNA encoding a CSL gene that is specifically upregulated during endosperm development in Guar seeds. They then expressed the gene in somatic embryos of soybean. Microsomal preparations of the transgenic soybean clearly exhibited a mannosyltransferase activity by transferring mannose from GDP-mannose to a β-mannase-digestable high-molecular-weight product. The authors termed this enzyme mannan synthase (ManS) although additional characterization of the product will be necessary to establish this term unambiguously.
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Dhugga K.S., Bareirro R., Whitten B., Stecca K., Hazebroek J., Randhawa G.S., Dolan M., Kinney A.J., Tomes D., Nichols S., Anderson P. Guar seed β-mannan synthase is a member of the cellulose synthase super gene family. Science. 303:2004;363-366 First evidence that a member of the CSL-gene family is involved in the synthesis of a wall polysaccharide other than cellulose. The authors cloned a cDNA encoding a CSL gene that is specifically upregulated during endosperm development in Guar seeds. They then expressed the gene in somatic embryos of soybean. Microsomal preparations of the transgenic soybean clearly exhibited a mannosyltransferase activity by transferring mannose from GDP-mannose to a β-mannase-digestable high-molecular-weight product. The authors termed this enzyme mannan synthase (ManS) although additional characterization of the product will be necessary to establish this term unambiguously.
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Science
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Dhugga, K.S.1
Bareirro, R.2
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Hazebroek, J.5
Randhawa, G.S.6
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40
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Perrin R.M., DeRocher A.E., Bar-Peled M., Zeng W., Norambuena L., Orellana A., Raikhel N.V., Keegstra K. Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall biosynthesis. Science. 284:1999;1976-1979
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Sarria R., Wagner T.A., O'Neill M.A., Faik A., Wilkerson C.G., Keegstra K., Raikhel N.V. Characterization of a family of Arabidopsis genes related to xyloglucan fucosyltransferase1. Plant Physiol. 127:2001;1595-1606
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Sarria, R.1
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42
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The mur2 mutant of Arabidopsis thaliana lacks fucosylated xyloglucan because of a lesion in fucosyltransferase AtFUT1
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The authors identify the gene that is affected in the mur2 mutant. MUR2 encodes a xyloglucan fucosyltransferase; the mutated form mur2 is inactive. The authors provide an in-depth analysis of the xyloglucan structure of mur2 plants, which indicates a 98% reduction in the fucosylation of xyloglucan but of no other class of wall components. Interestingly, no major mur2 phenotype was observed, indicating that xyloglucan fucosylation does not influence wall strength as was believed previously.
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Vanzin G.F., Madson M., Carpita N.C., Raikhel N.V., Keegstra K., Reiter W.D. The mur2 mutant of Arabidopsis thaliana lacks fucosylated xyloglucan because of a lesion in fucosyltransferase AtFUT1. Proc Natl Acad Sci USA. 99:2002;3340-3345 The authors identify the gene that is affected in the mur2 mutant. MUR2 encodes a xyloglucan fucosyltransferase; the mutated form mur2 is inactive. The authors provide an in-depth analysis of the xyloglucan structure of mur2 plants, which indicates a 98% reduction in the fucosylation of xyloglucan but of no other class of wall components. Interestingly, no major mur2 phenotype was observed, indicating that xyloglucan fucosylation does not influence wall strength as was believed previously.
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Proc Natl Acad Sci USA
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Vanzin, G.F.1
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Reiter, W.D.6
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43
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The authors gain further insights into the function of a fucosyltransferase that is involved in xyloglucan biosynthesis on a tissue level by comparing data from three analyses: an expression analysis of the corresponding gene, the determination of the enzyme activity and a structural analysis of xyloglucan using NMR spectroscopy. They used their conclusions from this comparison, together with the detailed analysis of an insertional T-DNA mutant and an overexpression line, to formulate novel hypotheses such as the influence of O-acetylation on xyloglucan fucosylation.
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Perrin R.M., Jia Z., Wagner T.A., O'Neill M.A., Sarria R., York W.S., Raikhel N.V., Keegstra K. Analysis of xyloglucan fucosylation in Arabidopsis. Plant Physiol. 132:2003;768-778 The authors gain further insights into the function of a fucosyltransferase that is involved in xyloglucan biosynthesis on a tissue level by comparing data from three analyses: an expression analysis of the corresponding gene, the determination of the enzyme activity and a structural analysis of xyloglucan using NMR spectroscopy. They used their conclusions from this comparison, together with the detailed analysis of an insertional T-DNA mutant and an overexpression line, to formulate novel hypotheses such as the influence of O-acetylation on xyloglucan fucosylation.
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Plant Physiol
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Perrin, R.M.1
Jia, Z.2
Wagner, T.A.3
O'Neill, M.A.4
Sarria, R.5
York, W.S.6
Raikhel, N.V.7
Keegstra, K.8
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44
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Pauly M., Eberhard S., Albersheim P., Darvill A., York W.S. Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells. Planta. 214:2001;67-74
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Pauly, M.1
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Lerouxel O., Choo T.S., Seveno M., Usadel B., Faye L., Lerouge P., Pauly M. Rapid structural phenotyping of plant cell wall mutants by enzymatic oligosaccharide fingerprinting. Plant Physiol. 130:2002;1754-1763
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Lerouxel, O.1
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Faye, L.5
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Pauly, M.7
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46
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0037963449
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The MUR3 gene of Arabidopsis encodes a xyloglucan galactosyltransferase that is evolutionarily related to animal exostosins
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The authors identify the gene affected in the mur3 mutant. MUR3 encodes a xyloglucan galacatosyltransferase that acts on a specific xylosyl residue. They provide an in-depth analysis of the xyloglucan structure of mur3, confirming the activity found in vitro. The MUR3 gene is a member of a large multi-gene family that is likely to contain many other genes that are candidates for roles in wall biosynthesis. Interesting possibilities include genes encoding a necessary second xyloglucan galactosyltransferase and a potential arabinosyltransferase that is involved in the synthesis of xyloglucan in the Solanaceae.
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Madson M., Dunand C., Li X., Verma R., Vanzin G.F., Caplan J., Shoue D.A., Carpita N.C., Reiter W.D. The MUR3 gene of Arabidopsis encodes a xyloglucan galactosyltransferase that is evolutionarily related to animal exostosins. Plant Cell. 15:2003;1662-1670 The authors identify the gene affected in the mur3 mutant. MUR3 encodes a xyloglucan galacatosyltransferase that acts on a specific xylosyl residue. They provide an in-depth analysis of the xyloglucan structure of mur3, confirming the activity found in vitro. The MUR3 gene is a member of a large multi-gene family that is likely to contain many other genes that are candidates for roles in wall biosynthesis. Interesting possibilities include genes encoding a necessary second xyloglucan galactosyltransferase and a potential arabinosyltransferase that is involved in the synthesis of xyloglucan in the Solanaceae.
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Plant Cell
, vol.15
, pp. 1662-1670
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Madson, M.1
Dunand, C.2
Li, X.3
Verma, R.4
Vanzin, G.F.5
Caplan, J.6
Shoue, D.A.7
Carpita, N.C.8
Reiter, W.D.9
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47
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Tensile properties of Arabidopsis cell walls depend on both a xyloglucan cross-linked microfibrillar network and rhamnogalacturonan II-borate complexes
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Ryden P., Sugimoto-Shirasu K., Smith A.C., Findlay K., Reiter W.D., McCann M.C. Tensile properties of Arabidopsis cell walls depend on both a xyloglucan cross-linked microfibrillar network and rhamnogalacturonan II-borate complexes. Plant Physiol. 132:2003;1033-1040
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Plant Physiol
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Ryden, P.1
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Smith, A.C.3
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McCann, M.C.6
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48
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An Arabidopsis gene encoding an alpha-xylosyltransferase involved in xyloglucan biosynthesis
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The authors clone a group of potential xyloglucan xylosyltransferase genes that were identified on the basis of an in vitro assay of pea microsomal fractions for a xyloglucan xylosyltransferase activity. The heterologous expression of these genes pointed out one gene that specifically transfers a xylosyl-residue to a cello-oligosaccharide chain, laying the foundation for more detailed studies of the xylosylation of xyloglucan.
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Faik A., Price N.J., Raikhel N.V., Keegstra K. An Arabidopsis gene encoding an alpha-xylosyltransferase involved in xyloglucan biosynthesis. Proc Natl Acad Sci USA. 99:2002;7797-7802 The authors clone a group of potential xyloglucan xylosyltransferase genes that were identified on the basis of an in vitro assay of pea microsomal fractions for a xyloglucan xylosyltransferase activity. The heterologous expression of these genes pointed out one gene that specifically transfers a xylosyl-residue to a cello-oligosaccharide chain, laying the foundation for more detailed studies of the xylosylation of xyloglucan.
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Proc Natl Acad Sci USA
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Faik, A.1
Price, N.J.2
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Keegstra, K.4
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49
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Edwards M.E., Dickson C.A., Chengappa S., Sidebottom C., Gidley M.J., Reid J.S. Molecular characterisation of a membrane-bound galactosyltransferase of plant cell wall matrix polysaccharide biosynthesis. Plant J. 19:1999;691-697
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Edwards M.E., Marshall E., Gidley M.J., Reid J.S.G. Transfer specificity of detergent-solubilized fenugreek galactomannan galactosyltransferase. Plant Physiol. 129:2002;1391-1397
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Edwards, M.E.1
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Tobacco transgenic lines that express fenugreek galactomannan galactosyltransferase constitutively have structurally altered galactomannans in their seed endosperm cell walls
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Reid J.S., Edwards M.E., Dickson C.A., Scott C., Gidley M.J. Tobacco transgenic lines that express fenugreek galactomannan galactosyltransferase constitutively have structurally altered galactomannans in their seed endosperm cell walls. Plant Physiol. 131:2003;1487-1495
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Plant Physiol
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Dickson, C.A.3
Scott, C.4
Gidley, M.J.5
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52
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0036801696
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Quasimodo1 encodes a putative membrane-bound glycosyltransferase required for normal pectin synthesis and cell adhesion in Arabidopsis
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The authors isolated the qua mutant, which exhibits a dwarfed phenotype and a cell-adhesion defect. Analysis of the cell walls of this mutant revealed a reduction in homogalacturonan, the major component of the pectic polysaccharides. QUA1 encodes a putative membrane-bound GT. Although the biochemical activity of QUA1 has not been shown yet, it seems to be the first promising candidate for a GT that is involved in the synthesis of pectins.
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Bouton S., Leboeuf E., Mouille G., Leydecker M.T., Talbotec J., Granier F., Lahaye M., Höfte H., Truong H.N. Quasimodo1 encodes a putative membrane-bound glycosyltransferase required for normal pectin synthesis and cell adhesion in Arabidopsis. Plant Cell. 14:2002;2577-2590 The authors isolated the qua mutant, which exhibits a dwarfed phenotype and a cell-adhesion defect. Analysis of the cell walls of this mutant revealed a reduction in homogalacturonan, the major component of the pectic polysaccharides. QUA1 encodes a putative membrane-bound GT. Although the biochemical activity of QUA1 has not been shown yet, it seems to be the first promising candidate for a GT that is involved in the synthesis of pectins.
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Plant Cell
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Bouton, S.1
Leboeuf, E.2
Mouille, G.3
Leydecker, M.T.4
Talbotec, J.5
Granier, F.6
Lahaye, M.7
Höfte, H.8
Truong, H.N.9
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53
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0037058926
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A pectin glucuronyltransferase gene is essential for intercellular attachment in the plant meristem
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The authors isolated a tobacco mutant (nolac-H18) that exhibits a severe defect in cell adhesion. The affected gene turns out to encode a putative membrane-bound GT (NpGUT1). A detailed analysis of the walls of the nolac-H18 mutant, in particular of the pectic polysaccharide RGII, provided evidence that NpGUT1 might be a glucuronsyl-transferase. In addition, the authors demonstrated that the structural alteration of RGII in the nolac-H18 mutant changes the RGII borate dimerization properties, which might be responsible for the cell-adhesion defect.
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Iwai H., Masaoka N., Ishii T., Satoh S. A pectin glucuronyltransferase gene is essential for intercellular attachment in the plant meristem. Proc Natl Acad Sci USA. 99:2002;16319-16324 The authors isolated a tobacco mutant (nolac-H18) that exhibits a severe defect in cell adhesion. The affected gene turns out to encode a putative membrane-bound GT (NpGUT1). A detailed analysis of the walls of the nolac-H18 mutant, in particular of the pectic polysaccharide RGII, provided evidence that NpGUT1 might be a glucuronsyl-transferase. In addition, the authors demonstrated that the structural alteration of RGII in the nolac-H18 mutant changes the RGII borate dimerization properties, which might be responsible for the cell-adhesion defect.
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Proc Natl Acad Sci USA
, vol.99
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Iwai, H.1
Masaoka, N.2
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Scheible W-R, Bashir S, Rose JKC: Plant cell walls in the post-genomic era. In Annual Plant Reviews, vol 8. The Plant Cell Wall. Edited by Rose JCK. Sheffield: Blackwell Publishing - CRC Press; 2003:325-375.
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Mouille G., Robin S., Lecomte M., Pagant S., Höfte H. Classification and identification of Arabidopsis cell wall mutants using Fourier-Transform InfraRed (FT-IR) microspectroscopy. Plant J. 35:2003;393-404
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Plant J
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Carpita C.C., McCann M.C. The functions of cell wall polysaccharides in composition and architecture revealed through mutations. Plant Soil. 247:2002;71-80
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Willats W.G.T., Rasmussen S.E., Kristensen T., Mikkelsen J.D., Knox J.P. Sugar-coated microarrays: a novel slide surface for the high-throughput analysis of glycans. Proteomics. 2:2002;1666-1671
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Desprez T., Vernhettes S., Fagard M., Refregier G., Desnos T., Aletti E., Py N., Pelletier S., Höfte H. Resistance against herbicide isoxaben and cellulose deficiency caused by distinct mutations in same cellulose synthase isoform CESA6. Plant Physiol. 128:2002;482-490
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Expression of a mutant form of cellulose synthase AtCesA7 causes dominant negative effect on cellulose biosynthesis
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The authors report the isolation of two fragile fiber (fra) Arabidopsis mutants, fra5 and fra6, which have point mutations in the AtCESA7 and AtCESA8 genes, respectively. Both homozygous mutants display reductions in the wall thickness of interfascicular fibers and the amount of cellulose, but the fra5 mutation is semidominant. Moreover, the constitutive overexpression of the fra5 allele in a wildtype background does not affect CESA7 gene expression. This overexpression does, however, aggravate phenotypes and leads to new phenotypes, including changes in plant morphology. These include the formation of a pendent stem, slight dwarfism, a reduction in the breaking strength of inflorescence stems, the appearance of collapsed xylem, and reduced stem-length caused by reduced length of pith cells. These results indicate that fra5 overexpression not only interferes with cellulose synthesis during secondary wall thickening but also affects cellulose synthesis during primary wall formation.
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Zhong R., Morrison W.H., Freshour G.D., Hahn M.G., Ye Z.H. Expression of a mutant form of cellulose synthase AtCesA7 causes dominant negative effect on cellulose biosynthesis. Plant Physiol. 132:2003;786-795 The authors report the isolation of two fragile fiber (fra) Arabidopsis mutants, fra5 and fra6, which have point mutations in the AtCESA7 and AtCESA8 genes, respectively. Both homozygous mutants display reductions in the wall thickness of interfascicular fibers and the amount of cellulose, but the fra5 mutation is semidominant. Moreover, the constitutive overexpression of the fra5 allele in a wildtype background does not affect CESA7 gene expression. This overexpression does, however, aggravate phenotypes and leads to new phenotypes, including changes in plant morphology. These include the formation of a pendent stem, slight dwarfism, a reduction in the breaking strength of inflorescence stems, the appearance of collapsed xylem, and reduced stem-length caused by reduced length of pith cells. These results indicate that fra5 overexpression not only interferes with cellulose synthesis during secondary wall thickening but also affects cellulose synthesis during primary wall formation.
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Plant Physiol
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AtCSLA7, a cellulose synthase-like putative glycosyltransferase, is important for pollen tube growth and embryogenesis in Arabidopsis
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Goubet F., Misrahi A., Park S.K., Zhang Z.N., Twell D., Dupree P. AtCSLA7, a cellulose synthase-like putative glycosyltransferase, is important for pollen tube growth and embryogenesis in Arabidopsis. Plant Physiol. 131:2003;547-557
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Identification of Arabidopsis rat mutants
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Zhu Y.M., Nam J., Humara J.M., Mysore K.S., Lee L.Y., Cao H.B., Valentine L., Li J.L., Kaiser A.D., Kopecky A.L., et al. Identification of Arabidopsis rat mutants. Plant Physiol. 132:2003;494-505
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KOJAK encodes a cellulose synthase-like protein required for root hair cell morphogenesis in Arabidopsis
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Favery B., Ryan E., Foreman J., Linstead P., Boudonck K., Steer M., Shaw P., Dolan L. KOJAK encodes a cellulose synthase-like protein required for root hair cell morphogenesis in Arabidopsis. Genes Dev. 15:2001;79-89
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Wang X., Cnops G., Vanderhaeghen R., De Block S., Van Montagu M., Van Lijsebettens M. AtCSLD3, a cellulose synthase-like gene important for root hair growth in Arabidopsis. Plant Physiol. 126:2001;575-586
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Faik A., Bar-Peled M., DeRocher A.E., Zeng W.Q., Perrin R.M., Wilkerson C., Raikhel N.V., Keegstra K. Biochemical characterization and molecular cloning of an alpha-1, 2-fucosyltransferase that catalyzes the last step of cell wall xyloglucan biosynthesis in pea. J Biol Chem. 275:2000;15082-15089
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Faik, A.1
Bar-Peled, M.2
Derocher, A.E.3
Zeng, W.Q.4
Perrin, R.M.5
Wilkerson, C.6
Raikhel, N.V.7
Keegstra, K.8
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67
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0036949462
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The cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene encoding a putative glucosidase II, an enzyme processing N-glycans during ER quality control
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Burn J.E., Hurley U.A., Birch R.J., Arioli T., Cork A., Williamson R.E. The cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene encoding a putative glucosidase II, an enzyme processing N-glycans during ER quality control. Plant J. 32:2002;949-960
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(2002)
Plant J
, vol.32
, pp. 949-960
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Burn, J.E.1
Hurley, U.A.2
Birch, R.J.3
Arioli, T.4
Cork, A.5
Williamson, R.E.6
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