4.8 Article

Intragenic complementation at the Lotus japonicus CELLULOSE SYNTHASE-LIKE D1 locus rescues root hair defects

Journal

PLANT PHYSIOLOGY
Volume 186, Issue 4, Pages 2037-2050

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/plphys/kiab204

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Funding

  1. Agriculture and Agri-Food Canada
  2. National Science and Engineering Research Council of Canada (NSERC) [3277A01, RGPIN-2018-06172]

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Root hair cells are crucial for nutrient uptake and defense in plants, with the gene CSLD1 playing a role in root hair development in the legume species Lotus japonicus. Multiple mutant alleles of Ljcsld1 result in varying root hair phenotypes, with certain mutations affecting root nodule symbiosis. Intragenic complementation is observed between alleles with mutations in different CSLD1 domains, suggesting modular function of CSLD1 during root hair development.
Root hair cells form the primary interface of plants with the soil environment, playing key roles in nutrient uptake and plant defense. In legumes, they are typically the first cells to become infected by nitrogen-fixing soil bacteria during root nodule symbiosis. Here, we report a role for the CELLULOSE SYNTHASE-LIKE D1 (CSLD1) gene in root hair development in the legume species Lotus japonicus. CSLD1 belongs to the cellulose synthase protein family that includes cellulose synthases and cellulose synthase-like proteins, the latter thought to be involved in the biosynthesis of hemicellulose. We describe 11 Ljcsld1 mutant alleles that impose either short (Ljcsld1-1) or variable (Ljcsld1-2 to 11) root hair length phenotypes. Examination of Ljcsld1-1 and one variable-length root hair mutant, Ljcsld1-6, revealed increased root hair cell wall thickness, which in Ljcsld1-1 was significantly more pronounced and also associated with a strong defect in root nodule symbiosis. Lotus japonicus plants heterozygous for Ljcsld1-1 exhibited intermediate root hair lengths, suggesting incomplete dominance. Intragenic complementation was observed between alleles with mutations in different CSLD1 domains, suggesting CSLD1 function is modular and that the protein may operate as a homodimer or multimer during root hair development.

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