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  • 1. Nishikubo, Nobuyuki
    et al.
    Awano, Tatsuya
    Banasiak, Alicja
    Bourquin, Veronica
    Ibatullin, Farid
    Funada, Ryo
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Hayashi, Takahisa
    Sundberg, Björn
    Mellerowicz, Ewa J.
    Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of tension wood fibers in poplar - A glimpse into the mechanism of the balancing act of trees2007In: Plant and Cell Physiology, ISSN 0032-0781, E-ISSN 1471-9053, Vol. 48, no 6, p. 843-855Article in journal (Refereed)
    Abstract [en]

    Tension wood is a specialized tissue of deciduous trees that functions in bending woody stems to optimize their position in space. Tension wood fibers that develop on one side of the stem have an increased potency to shrink compared with fibers on the opposite side, thus creating a bending moment. It is believed that the gelatinous (G) cell wall layer containing almost pure cellulose of tension wood fibers is pivotal to their shrinking. By analyzing saccharide composition and linkage in isolated G-layers of poplar, we found that they contain some matrix components in addition to cellulose, of which xyloglucan is the most abundant. Xyloglucan, xyloglucan endo-transglycosylase (XET) activity and xyloglucan endo-transglycosylase/hydrolase (XTH) gene products were detected in developing G-layers by labeling using CCRC-M1 monoclonal antibody, in situ incorporation of XXXG-SR and the polyclonal antibody to poplar PttXET16-34, respectively, indicating that xyloglucan is incorporated into the G-layer during its development. Moreover, several XTH transcripts were altered and were generally up-regulated in developing tension wood compared with normal wood. In mature G-fibers, XTH gene products were detected in the G-layers while the XET activity was evident in the adjacent S-2 wall layer. We propose that XET activity is essential for G-fiber shrinking by repairing xyloglucan cross-links between G- and S-2-layers and thus maintaining their contact. Surprisingly, XTH gene products and XET activity persisted in mature G-fibers for several years, suggesting that the enzyme functions after cell death repairing the cross-links as they are being broken during the shrinking process.

  • 2. Takahashi, Junko
    et al.
    Rudsander, Ulla J.
    KTH, School of Chemical Science and Engineering (CHE), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
    Hedenstrom, Mattias
    Banasiak, Alicja
    Harholt, Jesper
    Amelot, Nicolas
    Immerzeel, Peter
    Ryden, Peter
    Endo, Satoshi
    Ibatullin, Farid M.
    KTH, School of Chemical Science and Engineering (CHE), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
    Brumer, Harry
    KTH, School of Chemical Science and Engineering (CHE), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
    del Campillo, Elena
    Master, Emma R.
    Scheller, Henrik Vibe
    Sundberg, Bjorn
    Teeri, Tuula T.
    KTH, School of Chemical Science and Engineering (CHE), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
    Mellerowicz, Ewa J.
    KORRIGAN1 and its Aspen Homolog PttCel9A1 Decrease Cellulose Crystallinity in Arabidopsis Stems2009In: Plant and Cell Physiology, ISSN 0032-0781, E-ISSN 1471-9053, Vol. 50, no 6, p. 1099-1115Article in journal (Refereed)
    Abstract [en]

    KORRIGAN1 (KOR1) is a membrane-bound cellulase implicated in cellulose biosynthesis. PttCel9A1 from hybrid aspen (Populus tremula L. tremuloides Michx.) has high sequence similarity to KOR1 and we demonstrate here that it complements kor1-1 mutants, indicating that it is a KOR1 ortholog. We investigated the function of PttCel9A1/KOR1 in Arabidopsis secondary growth using transgenic lines expressing 35S::PttCel9A1 and the KOR1 mutant line irx2-2. The presence of elevated levels of PttCel9A1/KOR1 in secondary walls of 35S::PttCel9A1 lines was confirmed by in muro visualization of cellulase activity. Compared with the wild type, 35S::PttCel9A1 lines had higher trifluoroacetic acid (TFA)-hydrolyzable glucan contents, similar Updegraff cellulose contents and lower cellulose crystallinity indices, as determined by C-13 solid-state nuclear magnetic resonance (NMR) spectroscopy. irx2-2 mutants had wild-type TFA-hydrolyzable glucan contents, but reduced Updegraff cellulose contents and higher than wild-type cellulose crystallinity indices. The data support the hypothesis that PttCel9A1/KOR1 activity is present in cell walls, where it facilitates cellulose biosynthesis in a way that increases the amount of non-crystalline cellulose.

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