The methyl transfer enzyme PRMT5 of the amoeba protein arginine was modified by nitrosylation.

Methylation modification and nitric oxide-dependent nitrosylation modification are highly conservative protein translational modifications, both of which are involved in regulating many biological processes, including regulating abuteriological stress responses.
but the molecular mechanism of regulating non-biological coercion is not clear.
The zuo Jianru research group of the Institute of Genetics and Developmental Biology of the Chinese Academy of Sciences found that the proteomics study of nitrosylated protein arginine methyl transferase PRMT5 was modified by nitrosylation.
PRMT5 is a highly conservative enzyme in highly ethnonucleic organisms that catalyzs the bisymmetric methylation modification of arginine, whose substrates include the core members of the pre-mRNA clipping body.
biochemical and molecular genetic analysis showed that in response to absolutionary stress, NO regulated its methyl transferase activity, i.e. Cys-125 was necessary for PRMT5 to sense the NO signal through a specific nitrosyl modification of the 125th bit cysteine residue (Cys-125).
the nitrosylation modification of Cys-125 in PRMT5 methyl transferase enhances the level of bisymmetric methylation modification of arginine in plants, mediates the normal shearing of the coercive gene pre-mRNA, thus enhancing the plant's tolerance to coercion.
the above-mentioned study found that NO-mediated protein nitrosylation modification and protein methylation path to each other, so as to coordinate the molecular mechanism of plant antagonist non-biological coercion.
the above-mentioned research was carried out by the Research Group of Zuo Jianru of the Institute of Genetic Development, Cao Xiaofeng Research Group, Bao Shili Research Group and Kong Zhaosheng Research Group of the Institute of Microbiology of the Chinese Academy of Sciences.
paper was published online July 27 in the journal Molenal Cell.
Hu Jiliang, Zuo Jianru Research Group and Kong Zhaosheng Research Group jointly trained Postdoctoral Yang Huanjie as co-authors of the paper.
the research was funded by the National Natural Science Foundation of China, the Chinese Academy of Sciences Strategic Pilot Science and Technology Project, the National Key Laboratory for Plant Genomes, the China Postdoctoral Science Foundation and the Chinese Academy of Sciences.
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