The plant primary cell wall is a dynamic structure that exhibits considerable spatial and temporal variability in term of composition and organization, reflecting a balance between wall synthesis, deposition, reorganization and selective disassembly. This is achieved through the coordinated action of a battery of wall synthesizing and modifying enzymes that collectively provide a mechanism for regulating cell size, shape and cell-cell adhesion. Thus, selective modification of wall architecture is an integral part of processes as diverse as cellular growth, fruit softening, organ abscission, vascular differentiation and responses to pathogens (reviewed in Carpita and McCann, 2000).

One of the key interactions in the primary wall of dicotyledons is formed between cellulose and the hemicellulose xyloglucan, which together typically comprise about two thirds of the dry wall mass. Xyloglucan binds non-covalently to cellulose, coating and cross-linking adjacent cellulose microfibrils (McCann et al. 1992) and the resulting extensive xyloglucan-cellulose network is thought to act as the major tension-bearing structure in the primary wall. Xyloglucan metabolizing enzymes therefore represent a potentially important mechanism for controlling wall strength and extensibility, for example through the modification of load-bearing xyloglucan tethers.

Cleavage of load-bearing xyloglucan cross-links by hydrolytic enzymes might be a means of achieving rapid wall loosening; however, in the absence of significant wall synthesis and reinforcement, the net result would be a reduction in wall tensile strength, with an increased potential for disastrous structural failure. Thinning of the wall as cell expansion proceeded would further exacerbate this weakening. An alternative mechanism for cleaving structurally important xyloglucan polymers emerged from an early hypothesis that cell growth involves... an endotransglycosylase that transfers a portion of a polysaccharide to itself  (Albersheim 1976). Evidence of such enzymes, capable of splitting and reconnecting xyloglucan molecules in rapidly growing plant tissues, was originally described by two independent research groups. Fry and colleagues named the enzyme corresponding to this activity xyloglucan endotransglycosylase (XET) ( Smith and Fry 1991), while (Nishitani and Tominaga 1992) described the purification of a protein, with a similar activity, that they termed endoxyloglucan transferase (EXT, later redesignated EXGT). At the same time, and as part of a third independent line of research, a xyloglucan-specific endo-ß-1,4-glucanase, orxyloglucanase, from nasturtium seeds, involved in depolymerization of storage xyloglucans during germination, was shown to exhibit xyloglucan transglucosylase activity under certain conditions in vitro (Farkas et al. 1992, Fanutti et al. 1993). This contrasted with its known xyloglucan hydrolase activity and exemplifies an interesting distinction between transglycosylase or hydrolase activities detected in vitro, and enzymatic modes of actionin vivo.

As of 2002, following a meeting of several research groups working with these enzymes/genes, a new unifying nomenclature has been adopted.

 


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