An enzyme activity capable of endotransglycosylation of heteroxylan polysaccharides is present in plant primary cell walls
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  • 作者:Sarah L. Johnston (1)
    Roneel Prakash (1)
    Nancy J. Chen (2)
    Monto H. Kumagai (2) (6)
    Helen M. Turano (2)
    Janine M. Cooney (3)
    Ross G. Atkinson (1)
    Robert E. Paull (2)
    Roshan Cheetamun (4)
    Antony Bacic (4)
    David A. Brummell (5)
    Roswitha Schr?der (1)
  • 关键词:Cell wall ; Endoxylanase ; Heteroxylan ; Papaya ; Xylan endotransglycosylase
  • 刊名:Planta
  • 出版年:2013
  • 出版时间:January 2013
  • 年:2013
  • 卷:237
  • 期:1
  • 页码:173-187
  • 全文大小:1313KB
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  • 作者单位:Sarah L. Johnston (1)
    Roneel Prakash (1)
    Nancy J. Chen (2)
    Monto H. Kumagai (2) (6)
    Helen M. Turano (2)
    Janine M. Cooney (3)
    Ross G. Atkinson (1)
    Robert E. Paull (2)
    Roshan Cheetamun (4)
    Antony Bacic (4)
    David A. Brummell (5)
    Roswitha Schr?der (1)

    1. The New Zealand Institute for Plant and Food Research Limited, Mount Albert Research Centre, Private Bag 92169, Auckland, 1142, New Zealand
    2. Department of Tropical Plant and Soil Sciences, University of Hawaii at Manoa, 3190 Maile Way, Honolulu, HI, 96822-2279, USA
    6. XtremeSignPost Inc., Leucadia, CA, 92024, USA
    3. The New Zealand Institute for Plant and Food Research Limited, Ruakura Research Centre, Private Bag 3123, Hamilton, 3240, New Zealand
    4. ARC Centre of Excellence in Plant Cell Walls, School of Botany, University of Melbourne, Melbourne, VIC, 3010, Australia
    5. The New Zealand Institute for Plant and Food Research Limited, Food Industry Science Centre, Private Bag 11600, Palmerston North, 4442, New Zealand
文摘
Heteroxylans in the plant cell wall have been proposed to have a role analogous to that of xyloglucans or heteromannans, forming growth-restraining networks by interlocking cellulose microfibrils. A xylan endotransglycosylase has been identified that can transglycosylate heteroxylan polysaccharides in the presence of xylan-derived oligosaccharides. High activity was detected in ripe fruit of papaya (Carica papaya), but activity was also found in a range of other fruits, imbibed seeds and rapidly growing seedlings of cereals. Xylan endotransglycosylase from ripe papaya fruit used a range of heteroxylans, such as wheat arabinoxylan, birchwood glucuronoxylan and various heteroxylans from dicotyledonous primary cell walls purified from tomato and papaya fruit, as donor molecules. As acceptor molecules, the enzyme preferentially used xylopentaitol over xylohexaitol or shorter-length acceptors. Xylan endotransglycosylase was active over a broad pH range and could perform transglycosylation reactions up to 55?°C. Xylan endotransglycosylase activity was purified from ripe papaya fruit by ultrafiltration and cation exchange chromatography. Highest endotransglycosylase activity was identified in fractions that also contained high xylan hydrolase activity and correlated with the presence of the endoxylanase CpaEXY1. Recombinant CpaEXY1 protein transiently over-expressed in Nicotiana benthamiana leaves showed both endoxylanase and xylan endotransglycosylase activities in vitro, suggesting that CpaEXY1 is a single enzyme with dual activity in planta. Purified native CpaEXY1 showed two- to fourfold higher endoxylanase than endotransglycosylase activity, suggesting that CpaEXY1 may act primarily as a hydrolase. We propose that xylan endotransglycosylase activity (like xyloglucan and mannan endotransglycosylase activities) could be involved in remodelling or re-arrangement of heteroxylans of the cellulose-non-cellulosic cell wall framework.

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