Biosynthesis of non-cellulosic polysaccharides of plant cell walls |
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| Affiliation: | 1. Pain Mechanisms Laboratory, Department of Anesthesiology, Wake Forest University Health Sciences, Winston-Salem, NC, United States;2. Department of Physiology and Pharmacology, Wake Forest University Health Sciences, Winston-Salem, NC, United States;3. Silvio O. Conte Center for Oxytocin and Cognition, Center for Translational Neuroscience, Department of Psychiatry and Behavioral Sciences, Yerkes National Primate Research Center, Emory University, Atlanta, GA, United States;1. BioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, TX 76203, United States;2. Forage Genetics International, West Salem, WI 54669, United States;3. Center for Bioenergy Innovation (CBI), Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States;1. Centro de Estudio de Proteínas, Facultad de Biología, Universidad de la Habana, Cuba;2. Institute of Biochemistry and Molecular Biology, Department of Chemistry, Faculty for Mathematics Informatics and Natural Sciences, University of Hamburg, Germany;3. Elanco Animal Health, Greenfield, IN, USA;4. Centro de Inmunología Molecular, La Habana, Cuba;5. Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Germany |
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| Abstract: | Enzymes that make the polymer backbones of plant cell wall polysaccharides have proven to be recalcitrant to biochemical purification. Availability of mutational genetics and genomic tools paved the way for rapid progress in identifying genes encoding various cell wall glycan synthases. Mutational genetics, the primary tool used in unraveling cellulose biosynthesis, was ineffective in assigning function to any of the hemicellulosic, polymerizing glycan synthases. A combination of comparative genomics and functional expression in a heterologous system allowed identification of various cellulose synthase-like (Csl) sequences as being involved in the formation of β-1,4-mannan, β-1,4-glucan, and mixed-linked glucan. A number of xylose-deficient mutants have led to a variety of genes, none of which thus far possesses the motifs known to be conserved among polymerizing β-glycan synthases. Except for xylan synthase, which appears to be an agglomerate of proteins just like cellulose synthase, Golgi glycan synthases already identified suggest that the catalytic polypeptide by itself is sufficient for enzyme activity, most likely as a homodimer. Several of the Csl genes remain to be assigned a function. The possibility of the involvement of various Csl genes in making more than one product remains. |
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