Protein O-GlcNAcylation impairment caused by N-acetylglucosamine phosphate mutase deficiency leads to growth variations in Arabidopsis thaliana
Protein O-GlcNAcylation impairment caused by N-acetylglucosamine phosphate mutase deficiency leads to growth variations in Arabidopsis thaliana
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DOI:
10.1111/tpj.16156
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发表时间:
2023-03-09
期刊:
影响因子:
7.2
通讯作者:
Yin,Heng
中科院分区:
文献类型:
--
作者:
Jia,Xiaochen;Zhang,Hongyan;Yin,Heng
As an essential enzyme in the uridine diphosphate (UDP)‐GlcNAc biosynthesis pathway, the significant role ofN‐acetylglucosamine phosphate mutase (AGM) remains unknown in plants. In the present study, a functional plant AGM (AtAGM) was identified fromArabidopsis thaliana. AtAGM catalyzes the isomerization of GlcNAc‐1‐P and GlcNAc‐6‐P, and has broad catalytic activity on different phosphohexoses. UDP‐GlcNAc contents were significantly decreased inAtAGM T‐DNA insertional mutants, which caused temperature‐dependent growth defects in seedlings and vigorous growth in adult plants. Further analysis revealed that proteinO‐GlcNAcylation but notN‐glycosylation was dramatically impaired inAtagmmutants due to UDP‐GlcNAc shortage. Combined with the results fromO‐GlcNAcylation orN‐glycosylation deficient mutants, andO‐GlcNAcase inhibitor all suggested that proteinO‐GlcNAcylation impairment mainly leads to the phenotypic variations ofAtagmplants. In conclusion, based on the essential role in UDP‐GlcNAc biosynthesis, AtAGM is important for plant growth mainly via proteinO‐GlcNAcylation‐level regulation.