Synthesis, processing and export of cytoplasmic endo-ß-1,4-xylanase from barley aleurone during germination

article
We have identified the major endo-β-l,4-xylanase (XYN-1) in the aleurone of germinating barley grain, and show that it is expressed as a precursor of Mr 61 500 with both N- and C-terminal propeptides. XYN-1 is synthesized as an inactive enzyme in the cytoplasm, and only becomes active at a late stage of germination when the aleurone ceases to secrete hydrolases. A series of processing steps, mediated in part by aleurone cysteine endoproteases, yields a mature active enzyme of Mr 34 000. Processing and extracellular release of the mature enzyme coincide with the programmed cell death (PCD)-regulated disintegration of aleurone cells. We discuss the significance of delayed aleurone cell-wall degradation by endoxylanases in relation to the secretory capacity of the aleurone, and propose a novel role for aleurone PCD in facilitating the export of hydrolases. Chemicals/CAS: alpha-Amylase, EC 3.2.1.1; Cysteine Endopeptidases, EC 3.4.22.-; Endo-1,4-beta Xylanases, EC 3.2.1.8; Green Fluorescent Proteins, 147336-22-9; Hydrolases, EC 3.-; Indicators and Reagents; Luminescent Proteins; Plant Proteins; RNA Precursors; Starch, 9005-25-8; Xylosidases, EC 3.2.1.-
TNO Identifier
72511
ISSN
09607412
Source
The Plant Journal, 26(2), pp. 191-204.
Pages
191-204
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