Title
Endo-xyloglucan transferase, a new class of trasferase involved in cell-wall construction
 
author
Nishitani K
 
Issue
1995.
 
Publisher
J Plant Res 108: 137-148
 
Abstract
Cell shape in plants is constrained by cell walls, which are thick yet dynamic structures composed of crystalline cellulose microfibrils and matrix polymers. Xyloglucans are the principal component of the matrix polymers and bind tightly to the surface of cellulose microfibrils and thereby cross-link them to form an interwoven xyloglucan-cellulose network structure. Thus, cleavage and reconnection of the cross-links between xyloglucan molecules are required for the rearrangement of the cell wall architecture, the process essential for both cell wall expansion and the wall deposition occurring during cell growth and differentiation. Endoxyloglucan transferase (EXT) is a newly identified class of transferase that catalyzes molecular grafting between xyloglucan molecules. This enzyme catalyzes both endo-type splitting of a xyloglucan molecule and reconnection of a newly generated reducing terminus of the xyloglucan to the non-reducing terminus of another xyloglucan molecule, thereby mediating molecular grafting between xyloglucan cross-links in plant cell walls. Molecular cloning and sequencing of EXT-cDNAs derived from five different plant species including A. thaliana and V. angularis has revealed that the amino acid sequence of the mature protein is extensively conserved in the five different plant species, indicating that EXT protein is ubiquitous among higher plants. This structural study has also disclosed the presence of a group of xyloglucan related proteins (XRPs) with transferase activity in higher plants. Current data strongly suggest that these proteins are involved in a wide spectrum of physiological activities including cell wall expansion and deposition in growing cell walls.
 
Pdf
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Comment
XTH gene family, a review   http://www.springerlink.com/(rodc1f55lfyev4f2i1giu5ea)/app/home/contribution.asp?referrer=parent&backto=issue,19,19;journal,48,56;linkingpublicationresults,1:108924,1