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… 

Cellulose Synthesis and Its Regulation

This chapter highlights recent research progress towards understanding the mechanism of cellulose synthesis in Arabidopsis by using a combination of molecular genetics, live cell imaging, and spectroscopic tools.

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.

The Cellulase KORRIGAN Is Part of the Cellulose Synthase Complex1[W]

A multidisciplinary approach was used, including live cell imaging, gel filtration chromatography analysis, split ubiquitin assays in yeast, and bimolecular fluorescence complementation, to show that KOR1 is an integral part of the primary cell wall CSC in the plasma membrane, which suggests a role for Kor1 both in the synthesis of cellulose microfibrils and in the intracellular trafficking of CSCs.

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.

Prime Time for Cellulose

New work is discussed that reveals the identity of the lipid primer that initiates synthesis of the glucan chain, the primary constituent of cellulose, in plants that cannot survive without cellulose.

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).



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.

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

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.

Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants

Isolation of the IXR1 gene by map-based cloning revealed that it encodes the AtCESA3 isoform of cellulose synthase, a highly conserved region of the enzyme near the carboxyl terminus that is well separated from the proposed active site.