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RNA Methyltransferase METTL16's Protein Domains Have Differential Functional Effects on Cell Processes

ABSTRACT: RNA Methyltransferase METTL16's Protein Domains Have Differential Functional Effects on Cell Processes

PROVIDER: PRJNA897891 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22177937_1.fastq.gz	Fastqsanger.gz
	SRR22177938_1.fastq.gz	Fastqsanger.gz
	SRR22177939_1.fastq.gz	Fastqsanger.gz
	SRR22177940_1.fastq.gz	Fastqsanger.gz
	SRR22177941_1.fastq.gz	Fastqsanger.gz

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RNA Methyltransferase METTL16’s Protein Domains Have Differential Functional Effects on Cell Processes

Project description:METTL16, a human m6A RNA methyltransferase, contains multiple RNA binding domains and is known to modify U6 and MAT2A RNAs. Usingmutagensis, we generated HEK293 cell lines stabling expressing nutated or WT forms of METTL16 to dtermine the imapct these mutations have on cell processes after removal of endogenous METTL16. We performed bottom-up, untargeted data dependent proteomics analysison all five cell lines to determine the global changes in peptide/protein abdundances; we identified 200-300 statistically significant altered proteinscompared to the wild-type exogenous METTL16 clone.

2023-10-24 | PXD042242 | Pride

RNA Methyltransferase METTL16's Protein Domains Have Differential Functional Effects on Cell Processes

Project description:To investigate the cellular role of METTL16, we established HEK293 cell lines over expressing wild-type METTL16 or METTL16 methylation and RNA binding mutations. We then removed endogenous METTL16 from the cells using CRISPR. We then performed gene expression profiling analysis using data obtained from RNA-seq of the various cell lines.

2023-06-29 | GSE217192 | GEO

RNA Methyltransferase METTL16's Protein Domains Have Differential Functional Effects on Cell Processes.

Project description:METTL16, a human m6A RNA methyltransferase, is currently known for its modification of U6 and MAT2A RNAs. Several studies have identified additional RNAs to which METTL16 binds, however whether METTL16 modifies these RNAs is still in question. Moreover, a recent study determined that METTL16 contains more than one RNA-binding domain, leaving the importance of each individual RNA-binding domain unknown. Here we examined the effects of mutating the METTL16 protein in certain domains on overall cell processes. We chose to mutate the N-terminal RNA-binding domain, the methyltransferase domain, and the C-terminal RNA-binding domain. With these mutants, we identified changes in RNA-binding ability, protein and RNA expression, cell cycle phase occupancy, and proliferation. From the resulting changes in RNA and protein expression, we saw effects on cell cycle, metabolism, intracellular transport, and RNA processing pathways, which varied between the METTL16 mutant lines. We also saw significant effects on the G1 and S phase occupancy times and proliferative ability with some but not all the mutants. We have therefore concluded that while METTL16 may or may not m6A-modify all RNAs it binds, its binding (or lack of) has a significant outcome on a variety of cell processes.

| S-EPMC10378215 | biostudies-literature

The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention

Project description:Maintenance of the intracellular levels of the methyl donor S-adenosylmethionine (SAM) is essential for a wide variety of biological processes. We demonstrate that the N6-adenosine methyltransferase METTL16 regulates expression of MAT2A, which encodes the only SAM synthetase expressed in most cells. Upon SAM depletion by methionine starvation, cells induce MAT2A expression by enhanced splicing of a retained intron. Induction requires METTL16 and its methylation substrate, a vertebrate conserved hairpin (hp1) in the MAT2A 3´ UTR. Increasing METTL16 occupancy on the MAT2A 3´ UTR is sufficient to induce efficient splicing. We propose that under SAM-limiting conditions, METTL16 occupancy on hp1 increases due to inefficient enzymatic turnover, which in turn promotes MAT2A splicing. Interestingly, human and S. pombe METTL16 methylate the U6 spliceosomal snRNA at a sequence identical to hp1. These observations suggest that the conserved U6 snRNA methyltransferase evolved an additional function in vertebrates to regulate SAM homeostasis.

2017-05-18 | GSE90914 | GEO

Determine the methyltransferase activities of METTL16 via MeRIP-seq (m6A-seq)

Project description:METTL16 belongs to methyltransferase like (METTL) family and could install m6A marks on its substrates. Here, we uncover a tumor-promoting role of METTL16 in AML and LSC self-renewal. To explore the mechanism underlying the oncogenic function of METTL16 in AML, we performed m6A-seq and RNA-seq. Via integrated analysis of m6A-seq data and RNA-seq data, we identified two bona fide targets of METTL16, BCAT1 and BCAT2. METTL16 functions as an m6A methyltransferase to regulate expression of BCAT1 and BCAT2, which contribute to reprogramming of BCAA metabolism.

2023-01-12 | GSE189995 | GEO

RNA-seq in wild-type, METTL16-knockout, and METTL16 rescue NOMO-1 cells

2023-01-12 | GSE190044 | GEO

Determine the methyltransferase activities of METTL3, METTL14, and METTL16 via MeRIP-seq (m6A-seq)

Project description:All the three enzymes, METTL3, METTL14, and METTL16, belong to methyltransferase like (METTL) family and possess the ability to deposit N6-methyladenosine (m6A) in mRNA. Via immunofluorescence staining and wertern blotting, we discovered either METTL3 or METTL14 mainly localize in nuclear, but METTL16 localizes in both cytosol and nuclei. To compare the m6A methyltransferase activities of the three m6A 'writers' and better understand their differences, MeRIP-seq (m6A-seq) was conducted with poly(A) RNAs isolaed from HEK293T cells with METTL3, 14 and 16 knockout.

2021-10-28 | GSE182607 | GEO

METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs

Project description:N6-methyladenosine (m6A) is a highly dynamic RNA modification that has recently emerged as a key regulator of gene expression. While many m6A modifications are installed by the METTL3-METTL14 complex, others appear to be introduced independently, implying that additional human m6A methyltransferases remain to be identified. Using crosslinking and analysis of cDNA (CRAC), we reveal that the putative human m6A “writer” protein METTL16 binds to the U6 snRNA and other ncRNAs as well as numerous lncRNAs and pre-mRNAs. We demonstrate that METTL16 is responsible for N6-methylation of A43 of the U6 snRNA and identify the early U6 biogenesis factors La, LARP7 and the methylphosphate capping enzyme MEPCE as METTL16-interaction partners. Interestingly, A43 lies within an essential ACAGAGA box of U6 that base pairs with 5’ splice sites of pre-mRNAs during splicing, suggesting that METTL16-mediated modification of this site plays an important role in splicing regulation. The identification of METTL16 as an active m6A methyltransferase in human cells expands our understanding of the mechanisms by which the m6A landscape is installed on cellular RNAs.

2017-10-19 | GSE103948 | GEO

Determining the methyltransferase activities of METTL3, METTL14, and METTL16

Project description:Determining the methyltransferase activities of METTL3, METTL14, and METTL16

| PRJNA659033 | ENA

METTL16 promotes translation and lung tumorigenesis by sequestering cytoplasmic eIF4E2

Project description:METTL16 was previously identified as an m6A methyltransferase. In this study, we validated the cytoplasmic location of METTL16 and explored its function in the cytoplasm. We found that METTL16 promoted translation by sequestering eIF4E2, a translation initiation repressor, from the 5' cap structure.

2022-03-07 | GSE197915 | GEO

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