J. Biol. Chem., Vol. 268, Issue 34, 25364-25368, Dec, 1993
Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a novel class of glycosyltransferase that mediates molecular grafting between matrix polysaccharides in plant cell walls
K Okazawa, Y Sato, T Nakagawa, K Asada, I Kato, E Tomita and K Nishitani
Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Shiga, Japan.
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.
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