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The mechanism of cellulose synthesis has been studied by characterizing the motility of cellulose synthase complexes tagged with a fluorescent protein; however, this approach has been used exclusively on the hypocotyl of  Arabidopsis thaliana . Here we characterize cellulose synthase motility in the model grass,  Brachypodium distachyon . We generated lines in which  mEGFP  is fused N-terminal to  BdCESA3  or  BdCESA6  and which grew indistinguishably from the wild type (Bd21-3) and had dense fluorescent puncta at or near the plasma membrane. Measured with a particle tracking algorithm, the average speed of GFP-BdCESA3 particles in the mesocotyl was 164 ± 78 nm min −1  (error gives standard deviation [SD], n = 1451 particles). Mean speed in the root appeared similar. For comparison, average speed in the  A. thaliana  hypocotyl expressing GFP-AtCESA6 was 184 ± 86 nm min −1  (n = 2755). For  B. distachyon , we quantified root diameter and elongation rate in response to inhibitors of cellulose (dichlorobenylnitrile; DCB), microtubules (oryzalin), or actin (latrunculin B). Neither oryzalin nor latrunculin affected the speed of CESA complexes; whereas, DCB reduced average speed by about 50% in  B. distachyon  and by about 35% in  A. thaliana . Evidently, between these species, CESA motility is well conserved.

Imaging cellulose synthase motility during primary cell wall synthesis in the grass Brachypodium distachyon