| Literature DB >> 19398462 |
Junko Takahashi1, Ulla J Rudsander, Mattias Hedenström, Alicja Banasiak, Jesper Harholt, Nicolas Amelot, Peter Immerzeel, Peter Ryden, Satoshi Endo, Farid M Ibatullin, Harry Brumer, Elena del Campillo, Emma R Master, Henrik Vibe Scheller, Björn Sundberg, Tuula T Teeri, Ewa J Mellerowicz.
Abstract
KORRIGAN1 (KOR1) is a membrane-bound cellulase implicated in cellulose biosynthesis. PttCel9A1 from hybrid aspen (Populus tremula L. x 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 (13)C 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.Entities:
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Year: 2009 PMID: 19398462 DOI: 10.1093/pcp/pcp062
Source DB: PubMed Journal: Plant Cell Physiol ISSN: 0032-0781 Impact factor: 4.927