Further Studies of the Ability of Xyloglucan Oligosaccharides to Inhibit Auxin-Stimulated Growth

Augur, Christopher; Yu, Liping; Sakai, Keiichiro; Ogawa, Tomoya; Sînaÿ, Pierre; Darvill, Alan G.; Albersheim, Peter

doi:10.1104/pp.99.1.180

Cited by 64 publications

(22 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…6D). The pattern of transcript accumulation in the epidermal layer and its absence in the elongated stem tissue reinforce the hypothesis that ␣-L-fucosidase plays a role in the control of cell elongation by regulating the levels of bioactive fucosylated xyloglucan oligosaccharides generated within the growing cell wall (24). The localized accumulation of ␣-L-fucosidase mRNA in the highly dividing meristematic tissue (both root and shoot) may also be interpreted as its product's having a regulatory function.…”

Section: Cdna and Genomic Cloning Of The Gene Encoding An ␣-L-fucosidsupporting

confidence: 66%

Molecular Cloning and Pattern of Expression of an α-L-Fucosidase Gene from Pea Seedlings

Augur¹,

Stiefel

Darvill

et al. 1995

Journal of Biological Chemistry

View full text Add to dashboard Cite

␣-L-Fucosidase is a cell wall protein purified from pea (Pisum sativum) epicotyls. The ␣-L-fucosidase hydrolyzes terminal fucosyl residues from oligosaccharides of plant cell wall xyloglucan. ␣-L-Fucosidase may be an important factor in plant growth regulation, as it inactivates fucose-containing xyloglucan oligosaccharides that inhibit growth of pea stem segments. The amino acid sequences of the NH 2 -terminal region and one internal peptide were used to design redundant oligonucleotides that were utilized as primers in a polymerase chain reaction (PCR) with cDNA, generated from pea mRNA, as the template. A specific PCR amplification product containing 357 base pairs was isolated, cloned, and sequenced. The deduced amino acid sequence included the two peptides used to design the primers for PCR plus two other peptides obtained by proteinase digestion of ␣-L-fucosidase. No sequence homology to other ␣-L-fucosidases was apparent, although the NH 2 -terminal region is strongly homologous to Kunitz-type trypsin inhibitors. cDNA and genomic copies were isolated and sequenced. In pea, the gene is present in two or three copies. Its mRNA is present in roots, leaves, and elongating shoots. The spatial pattern of expression of the ␣-L-fucosidase was determined by in situ hybridization. Xyloglucan (XG)1 is a hemicellulosic polysaccharide present in the primary cell walls of all of the higher plants that have been examined. XG forms strong noncovalent bonds to cellulose microfibrils and is believed to strengthen the cell walls by cross-linking the microfibrils (1). XG appears to have a regulatory as well as a structural role, as there is evidence that XG oligosaccharides regulate the rate of plant cell growth (2-4). Indeed, fucosylated subunits of XG inhibit auxin-stimulated growth in pea stem segments (4 -7). These oligosaccharins (oligosaccharides with biological regulatory properties) have relatively strict structural requirements for activity, including a critical terminal fucosyl residue. Hydrolysis of the ␣-L-fucosidic bonds abolishes the growth-inhibiting activity of the XG oligosaccharides. Thus, we hypothesized that plants have an ␣-Lfucosidase that participates in the regulation of plant growth by controlling the concentration of fucosylated XG oligosaccharides. This hypothesis led to the demonstration that pea stems have a developmentally regulated ␣-L-fucosidase with the ability to cleave the fucosyl residue of XG oligosaccharides. Indeed, the ␣-L-fucosidase, which was shown to reside in the primary cell walls of pea stems, has been purified to homogeneity (5).cDNAs encoding ␣-L-fucosidases have previously been isolated from human (8, 9) and rat (10) livers. The human and rat liver ␣-L-fucosidases have subunit molecular masses of approximately 50,100 and 55,000 Da, respectively. Both of these ␣-Lfucosidases hydrolyze artificial substrates such as p-nitrophenyl-␣-L-fucoside and 4-methylumbelliferyl fucoside. Both of these fucosidases have broad aglycon specificities such that they hydrolyze ␣-1,2-, ␣-1,3-, ␣-1,...

show abstract

Section: Cdna and Genomic Cloning Of The Gene Encoding An ␣-L-fucosidsupporting

confidence: 66%

Molecular Cloning and Pattern of Expression of an α-L-Fucosidase Gene from Pea Seedlings

Augur¹,

Stiefel

Darvill

et al. 1995

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Xyloglucan metabolism is thought to have an important role in cell definition, cell expansion, and regulation of plant growth and development (7)(8)(9)(10)(11). Recently, it was reported that xyloglucan integration by xyloglucan endotransglycosylase in the cell wall suppresses cell elongation, whereas that of the xyloglucan oligosaccharide XXXG accelerates elongation (12).…”

mentioning

confidence: 99%

Purification, Characterization, Cloning, and Expression of a Novel Xyloglucan-specific Glycosidase, Oligoxyloglucan Reducing End-specific Cellobiohydrolase

Yaoi

Mitsuishi

2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

A novel oligoxyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH), with a molecular mass of 97 kDa and a pI of 6.1, was isolated from the fungus Geotrichum sp. M128. Analysis of substrate specificity using various xyloglucan oligosaccharide structures revealed that OXG-RCBH had exoglucanase activity. It recognized the reducing end of oligoxyloglucan and released two glucosyl residue segments from the main chain. The full-length cDNA encoding OXG-RCBH was cloned and sequenced, and it had a 2436-bp open reading frame encoding an 812-amino acid protein. The deduced protein showed ϳ35% identity to members of glycoside hydrolase family 74. The cDNA encoding OXG-RCBH was then expressed in Escherichia coli. Although the recombinant protein was expressed as an inclusion body, renaturation was successful, and enzymatically active recombinant OXG-RCBH was obtained.

show abstract

“…During cell expansion and development, partial disassembly of the network is required (8,9). Furthermore, xyloglucan metabolism is thought to have important roles in cell definition, cell expansion, and regulation of plant growth and development (1,4,17,18,31). For example, in the cell walls of the growing plant, xyloglucan oligosaccharides may provide positive-or negative-feedback control during cell elongation (25).…”

mentioning

confidence: 99%

Cloning and Characterization of Two Xyloglucanases from Paenibacillus sp. Strain KM21

Yaoi

Nakai

Kameda

et al. 2005

Appl Environ Microbiol

View full text Add to dashboard Cite

Two xyloglucan-specific endo-␤-1,4-glucanases (xyloglucanases [XEGs]), XEG5 and XEG74, with molecular masses of 40 kDa and 105 kDa, respectively, were isolated from the gram-positive bacterium Paenibacillus sp. strain KM21, which degrades tamarind seed xyloglucan. The genes encoding these XEGs were cloned and sequenced. Based on their amino acid sequences, the catalytic domains of XEG5 and XEG74 were classified in the glycoside hydrolase families 5 and 74, respectively. XEG5 is the first xyloglucanase belonging to glycoside hydrolase family 5. XEG5 lacks a carbohydrate-binding module, while XEG74 has an X2 module and a family 3 type carbohydrate-binding module at its C terminus. The two XEGs were expressed in Escherichia coli, and recombinant forms of the enzymes were purified and characterized. Both XEGs had endoglucanase active only toward xyloglucan and not toward Avicel, carboxymethylcellulose, barley ␤-1,3/1,4-glucan, or xylan. XEG5 is a typical endo-type enzyme that randomly cleaves the xyloglucan main chain, while XEG74 has dual endo-and exo-mode activities or processive endo-mode activity. XEG5 digested the xyloglucan oligosaccharide XXXG XXXG to produce XXXG, whereas XEG74 digestion of XXXGXXXG resulted in XXX, XXXG, and GXXXG, suggesting that this enzyme cleaves the glycosidic bond of unbranched Glc residues. Analyses using various oligosaccharide structures revealed that unique structures of xyloglucan oligosaccharides can be prepared with XEG74.

show abstract

Further Studies of the Ability of Xyloglucan Oligosaccharides to Inhibit Auxin-Stimulated Growth

Cited by 64 publications

References 19 publications

Molecular Cloning and Pattern of Expression of an α-L-Fucosidase Gene from Pea Seedlings

Molecular Cloning and Pattern of Expression of an α-L-Fucosidase Gene from Pea Seedlings

Purification, Characterization, Cloning, and Expression of a Novel Xyloglucan-specific Glycosidase, Oligoxyloglucan Reducing End-specific Cellobiohydrolase

Cloning and Characterization of Two Xyloglucanases from Paenibacillus sp. Strain KM21

Contact Info

Product

Resources

About