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Title: Biochemical and physiological flexibility accompanies reduced cellulose biosynthesis in Brachypodium cesa1S830N

Journal Article · · AoB Plants
 [1];  [2];  [1];  [3];  [4];  [5];  [2];  [4];  [6];  [1];
  1. Department of Horticulture, University of Kentucky, Lexington, KY, USA
  2. Department of Materials Science and Engineering, North Carolina State University, Raleigh, NC, USA
  3. Donald Danforth Plant Science Center, St. Louis, MO, USA, KWS Gateway Research Center, St. Louis, MO, USA
  4. Donald Danforth Plant Science Center, St. Louis, MO, USA
  5. Donald Danforth Plant Science Center, St. Louis, MO, USA, Syngenta Japan K.K., Chuo-ku, Tokyo, Japan
  6. Plant Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, NY, USA
+ Show Author Affiliations

Here, we present a study into the mechanisms of primary cell wall cellulose formation in grasses, using the model cereal grass Brachypodium distachyon. The exon found adjacent to the BdCESA1 glycosyltransferase QXXRW motif was targeted using Targeting Induced Local Lesions in Genomes (TILLING) and sequencing candidate amplicons in multiple parallel reactions (SCAMPRing) leading to the identification of the Bdcesa1S830N allele. Plants carrying this missense mutation exhibited a significant reduction in crystalline cellulose content in tissues that rely on the primary cell wall for biomechanical support. However, Bdcesa1S830N plants failed to exhibit the predicted reduction in plant height. In a mechanism unavailable to eudicotyledons, B. distachyon plants homozygous for the Bdcesa1S830N allele appear to overcome the loss of internode expansion anatomically by increasing the number of nodes along the stem. Stem biomechanics were resultantly compromised in Bdcesa1S830N. The Bdcesa1S830N missense mutation did not interfere with BdCESA1 gene expression. However, molecular dynamic simulations of the CELLULOSE SYNTHASE A (CESA) structure with modelled membrane interactions illustrated that Bdcesa1S830N exhibited structural changes in the translated gene product responsible for reduced cellulose biosynthesis. Molecular dynamic simulations showed that substituting S830N resulted in a stabilizing shift in the flexibility of the class specific region arm of the core catalytic domain of CESA, revealing the importance of this motion to protein function.

Research Organization:
Energy Frontier Research Centers (EFRC) (United States). Center for Lignocellulose Structure and Formation (CLSF); Pennsylvania State Univ., University Park, PA (United States)
Sponsoring Organization:
National Science Foundation (NSF); USDA; USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
SC0001090
OSTI ID:
1570542
Journal Information:
AoB Plants, Journal Name: AoB Plants Journal Issue: 5 Vol. 11; ISSN 2041-2851
Publisher:
Oxford University Press; Annals of Botany CompanyCopyright Statement
Country of Publication:
United Kingdom
Language:
English

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59 BASIC BIOLOGICAL SCIENCES
CESA
bio-inspired
biofuels (including algae and biomass)
biomechanics
carbon sequestration
cellular expansion
cellulose
class-specific region
materials and chemistry by design
membrane
molecular dynamics
synthesis (self-assembly)