Proteomics

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Impaired O-GlcNAcylation rather than N-glycosylation caused by AtAGM deficiency leads to growth variations in Arabidopsis thaliana


ABSTRACT: To reveal the function of N-acetylglucosamine phosphate mutase (AGM) and UDP-GlcNAc in Arabidopsis growth, WT and a T-DNA insertional mutant Atagm-2 were used for proteomic analysis.

ORGANISM(S): Arabidopsis Thaliana

SUBMITTER: Heng Yin  

PROVIDER: PXD024977 | iProX | Thu Mar 25 00:00:00 GMT 2021

REPOSITORIES: iProX

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Protein O-GlcNAcylation impairment caused by N-acetylglucosamine phosphate mutase deficiency leads to growth variations in Arabidopsis thaliana.

Jia Xiaochen X   Zhang Hongyan H   Qin Hongqiang H   Li Kuikui K   Liu Xiaoyan X   Wang Wenxia W   Ye Mingliang M   Yin Heng H  

The Plant journal : for cell and molecular biology 20230309 3


As an essential enzyme in the uridine diphosphate (UDP)-GlcNAc biosynthesis pathway, the significant role of N-acetylglucosamine phosphate mutase (AGM) remains unknown in plants. In the present study, a functional plant AGM (AtAGM) was identified from Arabidopsis 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 in AtAGM T-DNA insertional mutants, which caused te  ...[more]

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