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IGF2BP3 promotes mRNA degradation through internal m7G modification

ABSTRACT: IGF2BP3 promotes mRNA degradation through internal m7G modification

PROVIDER: PRJNA1006739 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25685500.fastq.gz	Fastqsanger.gz
	SRR25685459_1.fastq.gz	Fastqsanger.gz
	SRR25685459_2.fastq.gz	Fastqsanger.gz
	SRR25685460_1.fastq.gz	Fastqsanger.gz
	SRR25685460_2.fastq.gz	Fastqsanger.gz

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IGF2BP3 promotes mRNA degradation through internal m7G modification [seq_Ribo]

Project description:Recent studies have suggested that mRNA internal m7G and its writer protein METTL1 are closely related to cell metabolism and cancer regulation. Here, we identify that IGF2BP family proteins IGF2BP1-3 can preferentially bind internal mRNA m7G. Such interactions, especially IGF2BP3 with m7G, could promote the degradation of m7G target transcripts in cancer cells. IGF2BP3 is more responsive to changes of the m7G modification, while IGF2BP1 prefers m6A to stabilize the bound transcripts. We also demonstrate that p53 transcript, TP53, is m7G-modified at its 3’UTR in cancer cells. In glioblastoma, the methylation level and the half lifetime of the modified transcript could be modulated by tuning IGF2BP3, or by site-specific targeting of m7G through a dCas13b-guided system, resulting in modulation of cancer progression and chemosensitivity.

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Project description:The project aims to identify the RNA binding proteins that can specifically bind to mRNA internal modification N7-methylguanosine (m7G). N7-methylguanosine (m7G) methylation has been long identified as the essential cap modification for eukaryotic mRNA, but later has been identified internally in various types of RNAs, including tRNA, rRNA, miRNA, and mRNA. While the METTL1/WDR4 complex, responsible for tRNA m7G installation, has been suggested to be responsible for internal mRNA modification as well, little is known about the proteins that can identify and interact with m7G. To better understand its interaction with RNA binding proteins and further define its regulatory function in mRNA metabolism, we performed the experiment to pulldown proteins with different binding affinity on unmodified G and m7G and subject the enriched fractions to mass spectrometry.

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