A single amino-acid substitution at lysine 40 of an Arabidopsis thalianaα-tubulin causes extensive cell proliferation and expansion defects.
作者： Xue Xiong , Deyang Xu , Zhongnan Yang , Hai Huang , Xiaofeng Cui
DOI: 10.1111/JIPB.12003
关键词:
摘要: Microtubules are highly dynamic cytoskeletal polymers of α/β-tubulin heterodimers that undergo multiple post-translational modifications essential for various cellular functions in eukaryotes. The lysine 40 (K40) is largely conserved α-tubulins many eukaryote species, and the modification by acetylation at K40 critical neuronal development vertebrates. However, biological function plants remains unexplored. In this study, we show Arabidopsis thaliana constitutive expression mutated forms α-tubulin6 (TUA6) (TUA6(K40A) or TUA6(K40Q) ), which replaced alanine glutamine, result severely reduced plant size. Phenotypic characterization 35S:TUA6(K40A) transgenic revealed both cell proliferation expansion were affected. Cytological biochemical analyses showed accumulation α- β-tubulin proteins was significantly plants, cortical microtubule arrays disrupted, indicating α-tubulin maintaining stability. We also constructed 35S:TUA6(K40R) engineered TUA6 protein an arginine, found phenotypically indistinguishable from wild-type. Since arginine similar nature but cannot be acetylated, these results suggest a structural importance division expansion.
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