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@ARTICLE{Voiniciuc:819305,
      author       = {Voiniciuc, Cătălin and Zimmermann, Eva and Günl, Markus
                      and Fu, Lanbao and North, Helen M. and Usadel, Björn and
                      Schmidt, Maximilian},
      title        = {{E}xtensive {N}atural {V}ariation in {A}rabidopsis {S}eed
                      {M}ucilage {S}tructure},
      journal      = {Frontiers in Functional Plant Ecology},
      volume       = {7},
      issn         = {1664-462X},
      address      = {Lausanne},
      publisher    = {Frontiers Media88991},
      reportid     = {FZJ-2016-05006},
      pages        = {803},
      year         = {2016},
      abstract     = {Hydrated Arabidopsis thaliana seeds are coated by a
                      gelatinous layer called mucilage, which is mainly composed
                      of cell wall polysaccharides. Since mucilage is rich in
                      pectin, its architecture can be visualized with the
                      ruthenium red (RR) dye. We screened the seeds of around 280
                      Arabidopsis natural accessions for variation in mucilage
                      structure, and identified a large number of novel variants
                      that differed from the Col-0 wild-type. Most of the
                      accessions released smaller RR-stained capsules compared to
                      the Col-0 reference. By biochemically characterizing the
                      phenotypes of 25 of these accessions in greater detail, we
                      discovered that distinct changes in polysaccharide structure
                      resulted in gelatinous coatings with a deceptively similar
                      appearance. Monosaccharide composition analysis of total
                      mucilage extracts revealed a remarkable variation (from 50
                      to $200\%$ of Col-0 levels) in the content of galactose and
                      mannose, which are important subunits of heteromannan. In
                      addition, most of the natural variants had altered Pontamine
                      Fast Scarlet 4B staining of cellulose and significantly
                      reduced birefringence of crystalline structures. This
                      indicates that the production or organization of cellulose
                      may be affected by the presence of different amounts of
                      hemicellulose. Although, the accessions described in this
                      study were primarily collected from Western Europe, they
                      form five different phenotypic classes based on the combined
                      results of our experiments. This suggests that polymorphisms
                      at multiple loci are likely responsible for the observed
                      mucilage structure. The transcription of MUCILAGE-RELATED10
                      (MUCI10), which encodes a key enzyme for galactoglucomannan
                      synthesis, was severely reduced in multiple variants that
                      phenocopied the muci10-1 insertion mutant. Although, we
                      could not pinpoint any causal polymorphisms in this gene,
                      constitutive expression of fluorescently-tagged MUCI10
                      proteins complemented the mucilage defects of a muci10-like
                      accession. This leads us to hypothesize that some accessions
                      might disrupt a transcriptional regulator of MUCI10.
                      Therefore, this collection of publicly-available variants
                      should provide insight into plant cell wall organization and
                      facilitate the discovery of genes that regulate
                      polysaccharide biosynthesis.},
      cin          = {IBG-2},
      ddc          = {570},
      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:000377260700003},
      pubmed       = {pmid:27375657},
      doi          = {10.3389/fpls.2016.00803},
      url          = {https://juser.fz-juelich.de/record/819305},
}