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Doblin M.S., Vergara C.E., Read S.M., Newbigin E., and Bacic A. Plant cell wall biosynthesis: making the bricks. In: Rose J.K.C. (Ed). The Plant Cell Wall (2003), Blackwell Publishing Ltd 183-222
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Hayashi T., Yoshida K., Park Y.W., Konishi T., and Baba K. Cellulose metabolism in plants. In: Jeon K.W. (Ed). Int Rev Cytol Volume247 (2005), Academic Press 1-34
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Somerville C.R. Cellulose synthesis in higher plants. Annu Rev Cell Dev Biol 22 (2006) 53-78
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Scheible W.-R., and Pauly M. Glycosyltransferases and cell wall biosynthesis: novel players and insights. Curr Opin Plant Biol 7 (2004) 285-295
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Keegstra K., and Walton J. Plant science: β-glucans - brewer's bane, dietician's delight. Science 311 (2006) 1872-1873
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Djerbi S., Lindskog M., Arvestad L., Sterky F., and Teeri T. The genome sequence of black cottonwood Populus trichocarpa reveals 18 conserved cellulose synthase (CesA) genes. Planta 221 (2005) 739-746
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Joshi C.P., Bhandari S., Ranjan P., Kalluri U.C., Liang X., Fujino T., and Samuga A. Genomics of cellulose biosynthesis in poplars. New Phytol 164 (2004) 53-61
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Three loblolly pine CesA genes expressed in developing xylem are orthologous to secondary cell wall CesA genes of angiosperms
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Nairn C.J., and Haselkorn T. Three loblolly pine CesA genes expressed in developing xylem are orthologous to secondary cell wall CesA genes of angiosperms. New Phytol 166 (2005) 907-915
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Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains
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Kurek I., Kawagoe Y., Jacob-Wilk D., Doblin M., and 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
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Kurek, I.1
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Temperature-sensitive alleles of RSW2 link the KORRIGAN endo-1,4-β-glucanase to cellulose synthesis and cytokinesis in Arabidopsis
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Lane D.R., Wiedemeier A., Peng L., Höfte H., Vernhettes S., Desprez T., Hocart C.H., Birch R.J., Baskin T.I., Burn J.E., et al. Temperature-sensitive alleles of RSW2 link the KORRIGAN endo-1,4-β-glucanase to cellulose synthesis and cytokinesis in Arabidopsis. Plant Physiol 126 (2001) 278-288
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Lane, D.R.1
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Hocart, C.H.7
Birch, R.J.8
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Burn, J.E.10
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The irregular xylem 2 mutant is an allele of korrigan that affects the secondary cell wall of Arabidopsis thaliana
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Szyjanowicz P.M.J., McKinnon I., Taylor N.G., Gardiner J., Jarvis M.C., and Turner S.R. The irregular xylem 2 mutant is an allele of korrigan that affects the secondary cell wall of Arabidopsis thaliana. Plant J 37 (2004) 730-740
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Szyjanowicz, P.M.J.1
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Taylor, N.G.3
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Turner, S.R.6
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Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate guanylyltransferase and point to a requirement of N-linked glycosylation for cellulose biosynthesis
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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 USA 98 (2001) 2262-2267
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Lukowitz, W.1
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Glycosylphosphatidylinositol-anchored proteins are required for cell wall synthesis and morphogenesis in Arabidopsis
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Gillmor C.S., Lukowitz W., Brininstool G., Sedbrook J.C., Hamann T., Poindexter P., and Somerville C. Glycosylphosphatidylinositol-anchored proteins are required for cell wall synthesis and morphogenesis in Arabidopsis. Plant Cell 17 (2005) 1128-1140
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Gillmor, C.S.1
Lukowitz, W.2
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Poindexter, P.6
Somerville, C.7
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20
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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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Pagant S., Bichet A., Sugimoto K., Lerouxel O., Desprez T., McCann M., Lerouge P., Vernhettes S., and 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
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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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28444480365
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COBRA, an Arabidopsis extracellular glycosyl-phosphatidyl inositol-anchored protein, specifically controls highly anisotropic expansion through its involvement in cellulose microfibril orientation
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The authors identified and characterized a null mutant of the COBRA gene. The COBRA protein is an extracellular protein that is attached to the plasma membrane via a glycosyl-phosphatidyl inositol anchor. The cobra mutant has reduced levels of crystalline cellulose, and its remaining cellulose microfibrils are not properly organized. The authors conclude that the COBRA protein has an important role in the proper synthesis and/or orientation of cellulose microfibrils.
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Roudier F., Fernandez A.G., Fujita M., Himmelspach R., Borner G.H.H., Schindelman G., Song S., Baskin T.I., Dupree P., Wasteneys G.O., et al. COBRA, an Arabidopsis extracellular glycosyl-phosphatidyl inositol-anchored protein, specifically controls highly anisotropic expansion through its involvement in cellulose microfibril orientation. Plant Cell 17 (2005) 1749-1763. The authors identified and characterized a null mutant of the COBRA gene. The COBRA protein is an extracellular protein that is attached to the plasma membrane via a glycosyl-phosphatidyl inositol anchor. The cobra mutant has reduced levels of crystalline cellulose, and its remaining cellulose microfibrils are not properly organized. The authors conclude that the COBRA protein has an important role in the proper synthesis and/or orientation of cellulose microfibrils.
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(2005)
Plant Cell
, vol.17
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Roudier, F.1
Fernandez, A.G.2
Fujita, M.3
Himmelspach, R.4
Borner, G.H.H.5
Schindelman, G.6
Song, S.7
Baskin, T.I.8
Dupree, P.9
Wasteneys, G.O.10
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22
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27644451872
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Identification of novel genes in Arabidopsis involved in secondary cell wall formation using expression profiling and reverse genetics
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Microarray analysis of Arabidopsis tissues that are rich in secondary walls identifies a group of genes that exhibit patterns of expression resembling those of secondary wall CESA genes. Mutants in several of these genes constitute additional complementation groups of the irregular xylem (irx) series. A trio of novel irx alleles (irx7, irx8, and irx9) cause dramatic reductions in xylose, suggesting that the products of these alleles might be involved in xylan metabolism.
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Brown D.M., Zeef L.A.H., Ellis J., Goodacre R., and Turner S.R. Identification of novel genes in Arabidopsis involved in secondary cell wall formation using expression profiling and reverse genetics. Plant Cell 17 (2005) 2281-2295. Microarray analysis of Arabidopsis tissues that are rich in secondary walls identifies a group of genes that exhibit patterns of expression resembling those of secondary wall CESA genes. Mutants in several of these genes constitute additional complementation groups of the irregular xylem (irx) series. A trio of novel irx alleles (irx7, irx8, and irx9) cause dramatic reductions in xylose, suggesting that the products of these alleles might be involved in xylan metabolism.
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(2005)
Plant Cell
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, pp. 2281-2295
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Brown, D.M.1
Zeef, L.A.H.2
Ellis, J.3
Goodacre, R.4
Turner, S.R.5
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23
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20844445318
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Identification of genes required for cellulose synthesis by regression analysis of public microarray data sets
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Co-expression analysis of over 400 publicly available microarray datasets reveals groups of genes that exhibit co-regulation with CESA genes that are involved in primary or secondary wall biosynthesis. Mutants were characterized for a subset of candidate genes that are co-regulated with secondary wall CESA genes, and these plants displayed morphological and compositional alterations consistent with cell wall defects. Co-expression analysis provides a powerful means of identifying candidate genes whose products work together in a complex process.
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Persson S., Wei H., Milne J., Page G.P., and Somerville C.R. Identification of genes required for cellulose synthesis by regression analysis of public microarray data sets. Proc Natl Acad Sci USA 102 (2005) 8633-8638. Co-expression analysis of over 400 publicly available microarray datasets reveals groups of genes that exhibit co-regulation with CESA genes that are involved in primary or secondary wall biosynthesis. Mutants were characterized for a subset of candidate genes that are co-regulated with secondary wall CESA genes, and these plants displayed morphological and compositional alterations consistent with cell wall defects. Co-expression analysis provides a powerful means of identifying candidate genes whose products work together in a complex process.
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(2005)
Proc Natl Acad Sci USA
, vol.102
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Persson, S.1
Wei, H.2
Milne, J.3
Page, G.P.4
Somerville, C.R.5
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24
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33644924586
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Biosynthesis of cellulose-enriched tension wood in Populus: global analysis of transcripts and metabolites identifies biochemical and developmental regulators in secondary wall biosynthesis
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Tension wood in poplar has elevated levels of cellulose and greatly reduced levels of hemicellulose and lignin. In an effort to identify the regulatory changes responsible for the altered wood composition, microarray analysis was used to compare transcript levels in tissues producing normal wood with those in tissues producing tension wood. The authors found many interesting changes in the tissue producing tension wood, including dramatically increased levels of transcripts encoding the protein portion of certain arabinogalactan proteins. Interestingly, genes that are related to the cellulose biosynthetic machinery were not generally affected.
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Andersson-Gunnerås S., Mellerowicz E.J., Love J., Segerman B., Ohmiya Y., Coutinho P.M., Nilsson P., Henrissat B., Moritz T., and Sundberg B. Biosynthesis of cellulose-enriched tension wood in Populus: global analysis of transcripts and metabolites identifies biochemical and developmental regulators in secondary wall biosynthesis. Plant J 45 (2006) 144-165. Tension wood in poplar has elevated levels of cellulose and greatly reduced levels of hemicellulose and lignin. In an effort to identify the regulatory changes responsible for the altered wood composition, microarray analysis was used to compare transcript levels in tissues producing normal wood with those in tissues producing tension wood. The authors found many interesting changes in the tissue producing tension wood, including dramatically increased levels of transcripts encoding the protein portion of certain arabinogalactan proteins. Interestingly, genes that are related to the cellulose biosynthetic machinery were not generally affected.
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(2006)
Plant J
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Andersson-Gunnerås, S.1
Mellerowicz, E.J.2
Love, J.3
Segerman, B.4
Ohmiya, Y.5
Coutinho, P.M.6
Nilsson, P.7
Henrissat, B.8
Moritz, T.9
Sundberg, B.10
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25
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Bhandari S, Fujino T, Thammanagowda S, Zhang D, Xu F, Joshi CP: Xylem-specific and tension stress-responsive coexpression of KORRIGAN endoglucanase and three secondary wall-associated cellulose synthase genes in aspen trees. Planta 2006 in press. [Published on-line: DOI:10.1007/s00425-006-0269-1.]. In an effort to identify the regulatory changes responsible for the composition of tension wood, in situ hybridization was used to examine the expression of genes involved in cellulose biosynthesis: three CESA genes that are involved in secondary wall deposition and KORRIGAN. The authors found that expression of all four genes was significantly elevated on the upper side of bent stems where tension wood is formed and significantly reduced on the other side of the stem, which experienced compression stress. These results emphasize the importance of spatial control of wall biosynthetic genes.
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On the alignment of cellulose microfibrils by cortical microtubules: a review and a model
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Baskin T.I. On the alignment of cellulose microfibrils by cortical microtubules: a review and a model. Protoplasma 215 (2001) 150-171
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Baskin, T.I.1
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Visualization of cellulose synthase demonstrates functional association with microtubules
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The authors were able to visualize the movement of a CESA protein within Arabidopsis cells by complementing a CESA6 mutant (prc1-1) with a fluorescent-tagged version of CESA6. The protein, presumably as part of a rosette, moved within the plasma membrane in linear tracks that were aligned with cortical microtubules. Interestingly, the authors observed a significant pool of labeled CESA6 protein in the Golgi. This observation is consistent with the recent observation of CESA proteins in Golgi membranes during a proteomic analysis of Arabidopsis cellular compartments [30].
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Paredez A.R., Somerville C.R., and Ehrhardt D.W. Visualization of cellulose synthase demonstrates functional association with microtubules. Science 312 (2006) 1491-1495. The authors were able to visualize the movement of a CESA protein within Arabidopsis cells by complementing a CESA6 mutant (prc1-1) with a fluorescent-tagged version of CESA6. The protein, presumably as part of a rosette, moved within the plasma membrane in linear tracks that were aligned with cortical microtubules. Interestingly, the authors observed a significant pool of labeled CESA6 protein in the Golgi. This observation is consistent with the recent observation of CESA proteins in Golgi membranes during a proteomic analysis of Arabidopsis cellular compartments [30].
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Science
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Paredez, A.R.1
Somerville, C.R.2
Ehrhardt, D.W.3
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28
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The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane
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Valdivia R.H., and Schekman R. The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane. Proc Natl Acad Sci USA 100 (2003) 10287-10292
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Valdivia, R.H.1
Schekman, R.2
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An Arabidopsis endo-1,4-β-d-glucanase involved in cellulose synthesis undergoes regulated intracellular cycling
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The KORRIGAN gene encodes a membrane-bound endo-β-1,4-glucanase that is required for proper cellulose biosynthesis. Although the biochemical role of a glucanase during cellulose biosynthesis is not known, the authors investigated the intracellular location of the protein by complementing a korrigan mutant with a fluorescent-tagged version of KORRIGAN. Most of the resulting protein was located inside of the cell and it could not be detected on the plasma membrane. However, the behavior of the labeled protein during various treatments led the authors to conclude that the KORRIGAN protein undergoes regulated intracellular cycling during cellulose synthesis.
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Robert S., Bichet A., Grandjean O., Kierzkowski D., Satiat-Jeunemaitre B., Pelletier S., Hauser M.-T., Höfte H., and Vernhettes S. An Arabidopsis endo-1,4-β-d-glucanase involved in cellulose synthesis undergoes regulated intracellular cycling. Plant Cell 17 (2005) 3378-3389. The KORRIGAN gene encodes a membrane-bound endo-β-1,4-glucanase that is required for proper cellulose biosynthesis. Although the biochemical role of a glucanase during cellulose biosynthesis is not known, the authors investigated the intracellular location of the protein by complementing a korrigan mutant with a fluorescent-tagged version of KORRIGAN. Most of the resulting protein was located inside of the cell and it could not be detected on the plasma membrane. However, the behavior of the labeled protein during various treatments led the authors to conclude that the KORRIGAN protein undergoes regulated intracellular cycling during cellulose synthesis.
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Plant Cell
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Robert, S.1
Bichet, A.2
Grandjean, O.3
Kierzkowski, D.4
Satiat-Jeunemaitre, B.5
Pelletier, S.6
Hauser, M.-T.7
Höfte, H.8
Vernhettes, S.9
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Mapping the Arabidopsis organelle proteome
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Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T., Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C., et al. Mapping the Arabidopsis organelle proteome. Proc Natl Acad Sci USA 103 (2006) 6518-6523
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Dunkley, T.P.J.1
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Richmond T., and Somerville C. Integrative approaches to determining Csl function. Plant Mol Biol 47 (2001) 131-143
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Guar seed mannan synthase is a member of the cellulose synthase super gene family
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Dhugga K.S., Barreiro R., Whitten B., Hazebroek J., Randhawa G., Dolan M., Kinney A., Tomes D., Nichols S., and Anderson P. Guar seed mannan synthase is a member of the cellulose synthase super gene family. Science 16 (2004) 363-366
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Dhugga, K.S.1
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Dolan, M.6
Kinney, A.7
Tomes, D.8
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Expression of cellulose synthase-like (Csl) genes in insect cells reveals that CslA family members encode mannan synthases
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Heterologous expression of representative CSL proteins from Arabidopsis and rice in insect cells reveals that three CSLA genes from Arabidopsis encode β-1,4-glucomannan synthases. Despite the absence of an exogenous acceptor substrate, these proteins are active in vitro, indicating that mannan synthase does not require a plant-specific acceptor substrate for catalysis.
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Liepman A., Wilkerson C., 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 USA 102 (2005) 2221-2226. Heterologous expression of representative CSL proteins from Arabidopsis and rice in insect cells reveals that three CSLA genes from Arabidopsis encode β-1,4-glucomannan synthases. Despite the absence of an exogenous acceptor substrate, these proteins are active in vitro, indicating that mannan synthase does not require a plant-specific acceptor substrate for catalysis.
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Proc Natl Acad Sci USA
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Liepman, A.1
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Molecular characterisation of a membrane-bound galactosyltransferase of plant cell wall matrix polysaccharide biosynthesis
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Edwards M.E., Dickson C.A., Chengappa S., Sidebottom C., Gidley M.J., and 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., and Reid J.S.G. Transfer specificity of detergent-solubilized fenugreek galactomannan galactosyltransferase. Plant Physiol 129 (2002) 1391-1397
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The seeds of Lotus japonicus lines transformed with sense, antisense, and sense/antisense galactomannan galactosyltransferase constructs have structurally altered galactomannans in their endosperm cell walls
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Edwards M.E., Choo T.-S., Dickson C.A., Scott C., Gidley M.J., and Reid J.S.G. The seeds of Lotus japonicus lines transformed with sense, antisense, and sense/antisense galactomannan galactosyltransferase constructs have structurally altered galactomannans in their endosperm cell walls. Plant Physiol 134 (2004) 1153-1162
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