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@ARTICLE{Voiniciuc:856020,
      author       = {Voiniciuc, Catalin and Engle, Kristen A. and Günl, Markus
                      and Dieluweit, Sabine and Schmidt, Maximilian
                      Heinrich-Wilhelm and Yang, Jeong-Yeh and Moremen, Kelley W.
                      and Mohnen, Debra and Usadel, Björn},
      title        = {{I}dentification of {K}ey {E}nzymes for {P}ectin
                      {S}ynthesis in {S}eed {M}ucilage},
      journal      = {Plant physiology},
      volume       = {178},
      issn         = {1532-2548},
      address      = {Rockville, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-05705},
      pages        = {1045-1064},
      year         = {2018},
      abstract     = {Pectin is a vital component of the plant cell wall and
                      provides the molecular glue that maintains cell-cell
                      adhesion, among other functions. As the most complex wall
                      polysaccharide, pectin is composed of several covalently
                      linked domains, such as homogalacturonan (HG) and
                      rhamnogalacturonan I (RG I). Pectin has widespread uses in
                      the food industry and has emerging biomedical applications,
                      but its synthesis remains poorly understood. For instance,
                      the enzymes that catalyze RG I elongation remain unknown.
                      Recently, a coexpression- and sequence-based
                      MUCILAGE-RELATED (MUCI) reverse genetic screen uncovered
                      hemicellulose biosynthetic enzymes in the Arabidopsis
                      (Arabidopsis thaliana) seed coat. Here, we use an extension
                      of this strategy to identify MUCI70 as the founding member
                      of a glycosyltransferase family essential for the
                      accumulation of seed mucilage, a gelatinous wall rich in
                      unbranched RG I. Detailed biochemical and histological
                      characterization of two muci70 mutants and two
                      galacturonosyltransferase11 (gaut11) mutants identified
                      MUCI70 and GAUT11 as required for two distinct RG I domains
                      in seed mucilage. We demonstrate that, unlike MUCI70, GAUT11
                      catalyzes HG elongation in vitro and, thus, likely is
                      required for the synthesis of an HG region important for RG
                      I elongation. Analysis of a muci70 gaut11 double mutant
                      confirmed that MUCI70 and GAUT11 are indispensable for the
                      production and release of the bulk of mucilage RG I and for
                      shaping the surface morphology of seeds. In addition, we
                      uncover relationships between pectin and hemicelluloses and
                      show that xylan is essential for the elongation of at least
                      one RG I domain.},
      cin          = {ICS-7 / IBG-2},
      ddc          = {580},
      cid          = {I:(DE-Juel1)ICS-7-20110106 / I:(DE-Juel1)IBG-2-20101118},
      pnm          = {552 - Engineering Cell Function (POF3-552) / 582 - Plant
                      Science (POF3-582) / 583 - Innovative Synergisms (POF3-583)},
      pid          = {G:(DE-HGF)POF3-552 / G:(DE-HGF)POF3-582 /
                      G:(DE-HGF)POF3-583},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30228108},
      UT           = {WOS:000450014300012},
      doi          = {10.1104/pp.18.00584},
      url          = {https://juser.fz-juelich.de/record/856020},
}