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@ARTICLE{Voiniciuc:279645,
author = {Voiniciuc, Catalin and Günl, Markus and Schmidt,
Maximilian and Usadel, Björn},
title = {{H}ighly {B}ranched {X}ylan {M}ade by {IRREGULAR} {XYLEM}14
and {MUCILAGE}-{RELATED}21 {L}inks {M}ucilage to
{A}rabidopsis {S}eeds},
journal = {Plant physiology},
volume = {169},
number = {4},
issn = {0032-0889},
address = {Rockville, Md.},
publisher = {Soc.},
reportid = {FZJ-2015-07529},
pages = {2481-2495},
year = {2015},
abstract = {All cells of terrestrial plants are fortified by walls
composed of crystalline cellulose microfibrils and a variety
of matrix polymers. Xylans are the second most abundant type
of polysaccharides on Earth. Previous studies of Arabidopsis
(Arabidopsis thaliana) irregular xylem (irx) mutants, with
collapsed xylem vessels and dwarfed stature, highlighted the
importance of this cell wall component and revealed multiple
players required for its synthesis. Nevertheless, xylan
elongation and substitution are complex processes that
remain poorly understood. Recently, seed coat epidermal
cells were shown to provide an excellent system for
deciphering hemicellulose production. Using a coexpression
and sequence-based strategy, we predicted several
MUCILAGE-RELATED (MUCI) genes that encode
glycosyltransferases (GTs) involved in the production of
xylan. We now show that MUCI21, a member of an
uncharacterized clade of the GT61 family, and IRX14 (GT43
protein) are essential for the synthesis of highly branched
xylan in seed coat epidermal cells. Our results reveal that
xylan is the most abundant xylose-rich component in
Arabidopsis seed mucilage and is required to maintain its
architecture. Characterization of muci21 and irx14 single
and double mutants indicates that MUCI21 is a
Golgi-localized protein that likely facilitates the addition
of xylose residues directly to the xylan backbone. These
unique branches seem to be necessary for pectin attachment
to the seed surface, while the xylan backbone maintains
cellulose distribution. Evaluation of muci21 and irx14
alongside mutants that disrupt other wall components
suggests that mucilage adherence is maintained by complex
interactions between several polymers: cellulose, xylans,
pectins, and glycoproteins.},
cin = {IBG-2},
ddc = {580},
cid = {I:(DE-Juel1)IBG-2-20101118},
pnm = {582 - Plant Science (POF3-582)},
pid = {G:(DE-HGF)POF3-582},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000368472700011},
pubmed = {pmid:26482889},
doi = {10.1104/pp.15.01441},
url = {https://juser.fz-juelich.de/record/279645},
}