On December 31, 2022, Zhang, Guoqiang; Xu, Yongru; Wang, Xiaona; Zhu, Yuanxiang; Wang, Liangliang; Zhang, Wenxin; Wang, Yiru; Gao, Yajie; Wu, Xuna; Cheng, Ying; Sun, Qinmiao; Chen, Dahua published an article.Application In Synthesis of N-Methyl-7H-purin-6-amine The title of the article was Dynamic FMR1 granule phase switch instructed by m6A modification contributes to maternal RNA decay. And the article contained the following:
Maternal RNA degradation is critical for embryogenesis and is tightly controlled by maternal RNA-binding proteins. Fragile X mental-retardation protein (FMR1) binds target mRNAs to form ribonucleoprotein (RNP) complexes/granules that control various biol. processes, including early embryogenesis. However, how FMR1 recognizes target mRNAs and how FMR1-RNP granule assembly/disassembly regulates FMR1-associated mRNAs remain elusive. Here we show that Drosophila FMR1 preferentially binds mRNAs containing m6A-marked “AGACU” motif with high affinity to contributes to maternal RNA degradation The high-affinity binding largely depends on a hydrophobic network within FMR1 KH2 domain. Importantly, this binding greatly induces FMR1 granule condensation to efficiently recruit unmodified mRNAs. The degradation of maternal mRNAs then causes granule de-condensation, allowing normal embryogenesis. Our findings reveal that sequence-specific mRNAs instruct FMR1-RNP granules to undergo a dynamic phase-switch, thus contributes to maternal mRNA decay. This mechanism may represent a general principle that regulated RNP-granules control RNA processing and normal development. The experimental process involved the reaction of N-Methyl-7H-purin-6-amine(cas: 443-72-1).Application In Synthesis of N-Methyl-7H-purin-6-amine
The Article related to methyladenosine modification fmr phase switch rna decay, Placeholder for records without volume info and other aspects.Application In Synthesis of N-Methyl-7H-purin-6-amine
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