Sitosterol-β-glucoside as Primer for Cellulose Synthesis in Plants

  title={Sitosterol-$\beta$-glucoside as Primer for Cellulose Synthesis in Plants},
  author={Liangcai Peng and Yasushi Kawagoe and Pat Hogan and Deborah Pierson Delmer},
  pages={147 - 150}
Cellulose synthesis in plants requires β-1,4-glucan chain initiation, elongation, and termination. The process of chain elongation is likely to be distinct from the process of chain initiation. We demonstrate that a CesA glucosyltransferase initiates glucan polymerization by using sitosterol-β-glucoside (SG) as primer. Cotton fiber membranes synthesize sitosterol-cellodextrins (SCDs) from SG and uridine 5′-diphosphate–glucose (UDP-Glc) under conditions that also favor cellulose synthesis. The… 
Characterization of Cellulose Synthesis in Plant Cells
This review article covers the current knowledge about the cellulose biosynthesis-related gene family and various proteins like the KORRIGAN, sucrose synthase, cytoskeletal components, and COBRA-like proteins that have been involved in cellulOSE biosynthesis.
Cellulose synthases and synthesis in Arabidopsis.
The identified tentative interaction partners for the CesAs and shown that the migratory patterns of the CesA complexes depend on phosphorylation status may become good platforms for expanding the knowledge about cellulose synthesis in the near future.
Emerging Roles of β-Glucanases in Plant Development and Adaptative Responses
Plant β-glucanases are enzymes involved in the synthesis, remodelling and turnover of cell wall components during multiple physiological processes. Based on the type of the glycoside bond they
Phylogenetic Analysis of the Plant Endo-β-1,4-Glucanase Gene Family
Phylogenetic analysis of the endo-β-1,4-glucanase gene family of Arabidopsis and other plants revealed a clear distinction in three subfamilies (α, β, and γ), and it is suggested that these might also have a role in cellulose synthesis.
Functional reconstitution of cellulose synthase in Escherichia coli.
It is shown that cellulose-synthesizing activity is successfully reconstituted in Escherichia coli by expressing the bacterial cellulose synthase complex of Gluconacetobacter xylinus: CesA and CesB (formerly BcsA and BcsB, respectively).
Biochemical control of xylan biosynthesis - which end is up?
The lipid origin of cellulose.
In vitro synthesis of (1→3)-β-D-glucan (callose) and cellulose by detergent extracts of membranes from cell suspension cultures of hybrid aspen
The results presented show that the hybrid aspen is a promising model for in vitro studies on callose and cellulose synthesis, and was the only product synthesized when CHAPS extracts were used as a source of enzyme.


Unusual β-D-Xylosides That Prime Glycosaminoglycans in Animal Cells*
Interestingly, benzyl-β-D-threo-pentopyranos-4-uloside (4-keto derivative) and benzyl -4-methyl- β- D-xyloside, with a methyl group in place of an axial hydrogen at C-4, primed GAG chains, which suggests the possibility of designing inhibitors of GAG synthesis based on xylosides with reactive groups in key positions.
In vitro synthesis of a microfibrillar (1→3)-β-glucan by a ryegrass (Lolium multiflorum) endosperm (1→3)-β-glucan synthase enriched by product entrapment
The product-entrapped enzyme preparation contains six major polypeptides, and comparison of the SDS—PAGE pattern of this fraction with thepolypeptide profile of an immunoprecipitated (1→3)-β-glucan synthase preparation suggests that polypePTides at 30–31 and 55–58 kDa are the most likely candidates for participation in (1–3)- β- glucan synthesis.
The experimental herbicide CGA 325'615 inhibits synthesis of crystalline cellulose and causes accumulation of non-crystalline beta-1,4-glucan associated with CesA protein.
Developing cotton (Gossypium hirsutum) fibers, cultured in vitro with their associated ovules, were used to compare the effects of two herbicides that inhibit cellulose synthesis:
Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose.
The "parallel-up" packing in cellulose Ialpha and Ibeta unit cells was experimentally demonstrated by a combination of direct-staining the reducing ends of cellulose chains and
CELLULOSE BIOSYNTHESIS: Exciting Times for A Difficult Field of Study.
  • D. Delmer
  • Biology, Chemistry
    Annual review of plant physiology and plant molecular biology
  • 1999
Genetic evidence now supports the concept that members of this family encode the catalytic subunit of the cellulose synthase in these organisms, with various members showing tissue-specific expression.
Chitin oligosaccharide synthesis by rhizobia and zebrafish embryos starts by glycosyl transfer to O4 of the reducing-terminal residue.
The results indicate that prenylpyrophosphate-linked intermediates are not involved in the chitin oligosaccharide synthesis pathway, and shows that the use of artificial glycosyl acceptors such as pNPGlcNAc has not previously been described for a processiveglycosyltransferase.
Role of the putative membrane-bound endo-1,4-beta-glucanase KORRIGAN in cell elongation and cellulose synthesis in Arabidopsis thaliana.
It is demonstrated that the product of this gene is required for cellulose synthesis, which encodes a putative membrane-bound endo-1,4-beta-glucanase in KORRIGAN.
Molecular Directionality of Polysaccharide Polymerization by thePasteurella multocida Hyaluronan Synthase*
It is shown here that a HA synthase, PmHAS, from Gram-negative P. multocida bacteria polymerizes the HA chain by the addition of sugar units to the nonreducing terminus, and the fidelity of the individual sugar transfer reactions is sufficient to generate the authentic repeating structure of HA.
Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-beta-glucanase heterologously expressed in Pichia pastoris.
The functional analysis of Delta(1-90)Cel16, the N terminally truncated Cel16, missing residues 1 through 90 and comprising the catalytic domain of Cel16 expressed recombinantly in the methylotrophic yeast Pichia pastoris as a soluble protein, showed that Delta( 1-90)-hydrolyzed carboxymethylcellulose is a true endo-acting glucanase.