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Plant J ; 68(6): 941-53, 2011 Dec.
Article in English | MEDLINE | ID: mdl-21883548

ABSTRACT

The seeds of Arabidopsis thaliana and many other plants are surrounded by a pectinaceous mucilage that aids in seed hydration and germination. Mucilage is synthesized during seed development within maternally derived seed coat mucilage secretory cells (MSCs), and is released to surround the seed upon imbibition. The FEI1/FEI2 receptor-like kinases and the SOS5 extracellular GPI-anchored protein were shown previously to act on a pathway that regulates the synthesis of cellulose in Arabidopsis roots. Here, we demonstrate that both FEI2 and SOS5 also play a role in the synthesis of seed mucilage. Disruption of FEI2 or SOS5 leads to a reduction in the rays of cellulose observed across the seed mucilage inner layer, which alters the structure of the mucilage in response to hydration. Mutations in CESA5, which disrupts an isoform of cellulose synthase involved in primary cell wall synthesis, result in a similar seed mucilage phenotype. The data indicate that CESA5-derived cellulose plays an important role in the synthesis and structure of seed coat mucilage and that the FEI2/SOS5 pathway plays a role in the regulation of cellulose synthesis in MSCs. Moreover, these results establish a novel structural role for cellulose in anchoring the pectic component of seed coat mucilage to the seed surface.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Cellulose/biosynthesis , Genes, Plant , Glucosyltransferases/metabolism , Pectins/metabolism , Seeds/metabolism , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Biosynthetic Pathways , Gene Expression , Glucosyltransferases/genetics , Mutation , Plant Roots/growth & development , Protein Serine-Threonine Kinases/genetics , Protein Serine-Threonine Kinases/metabolism , Receptors, Cell Surface/genetics , Receptors, Cell Surface/metabolism
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