Reference "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a novel class of glycosyltransferase that mediates molecular grafting between matrix polysaccharides in plant cell walls"

Reference ID

9222

Title

Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a novel class of glycosyltransferase that mediates molecular grafting between matrix polysaccharides in plant cell walls

Source

The Journal of biological chemistry, 1993, vol. 268, pp. 25364-25368

Authors (7)

Okazawa-K	Sato-Y
Nakagawa-T	Asada-K
Kato-I	Tomita-E
Nishitani-K

Abstract

Endoxyloglucan transferase is a novel class of glycosyltransferase recently
purified from Vigna angularis (Nishitani, K,, and Tominaga, R. (1992) J. Biol.
Chem. 267, 21058-21064). This enzyme is the first transferase identified that
catalyzes molecular grafting between polysaccharide cross-links in the cell wall
matrix and participates in reconstruction of the network structure in the cell
wall. Based on the NH2-terminal amino acid sequence information of the purified
transferase, we have here cloned and sequenced cDNAs derived from five different
plant species, V. angularis, Triticum aestivum, Arabidopsis thaliana,
Lycopersicon esculentum, and Glycine max. In the five plant species, the amino
acid sequence of the mature proteins is conserved in the range of 71-90%
throughout their length. The consensus sequence for N-linked glycosylation, and
four cysteine residues are all conserved in the five species. Thus, the
endoxyloglucan transferase protein is ubiquitous among higher plants. The highly
conserved DNA sequence will serve as a promising tool for exploring the
molecular process by which cell wall construction, and hence cell growth, is
regulated.