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Characterization of METTL9-mediated methylation of DNAJB12

ABSTRACT: The analysis is part of a study aimed at characterizing a new human histidine-specific methyltransferase denoted METTL9. The putative METTL9 substrate DNAJB12 was immunoprecipitated from HEK293 cells and its PTM status was assessed by LC-MSMS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Magnus Jakobsson

LAB HEAD: Magnus E Jakobsson

PROVIDER: PXD020010 | Pride | 2020-11-19

REPOSITORIES: Pride

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			Action	DRS
	200609_Sample4_OsloIPHme_45kRes.raw	Raw
	200609_Sample8_OsloIPHme_45kRes.raw	Raw
	SEARCH.zip	Other

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Characterization of HAP-1 METTL9 KO cells

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Global analyses of endonucleolytic cleavage in mammals reveal expanded repertoires of cleavage-inducing small RNAs and their targets

Project description:In mammals, small RNAs are important players in post-transcriptional gene regulation. While their roles in mRNA destabilization and translational repression are well appreciated, their involvement in endonucleolytic cleavage of target RNAs is poorly understood. Very few microRNAs are known to guide RNA cleavage. Endogenous small interfering RNAs are expected to induce target cleavage, but their target genes remain largely unknown. We report a systematic study of small RNA-mediated endonucleolytic cleavage in mouse through integrative analysis of small RNA and degradome sequencing data without imposing any bias towards known small RNAs. Hundreds of small cleavage-inducing RNAs and their cognate target genes were identified, significantly expanding the repertoire of known small RNA-guided cleavage events. Strikingly, both small RNAs and their target sites demonstrated significant overlap with retrotransposons, providing evidence for the long-standing speculation that retrotransposable elements in mRNAs are leveraged as signals for gene targeting. Furthermore, our analysis showed that the RNA cleavage pathway is also present in human cells but affecting a different repertoire of retrotransposons. These results show that small RNA-guided cleavage is more widespread than previously appreciated. Their impact on retrotransposons in non-coding regions shed light on important aspects of mammalian gene regulation. Small RNA sequencing libraries were generated for H1, mouse whole brain at developmental stage E10 as well as mouse testis and cerebellum developmental stages E14, E18, post-natal 3 weeks, and post-natal 6 months

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METTL9 methylates H2B a-N-proline and suppresses human retrotransposition

Project description:The methylation of residues within histones plays a central role in regulating genome function; however, little is known about the biological importance of a-N-terminal histone methylation. Here we explored the function of the previously uncharacterized a-N methylation of mammalian histone 2B proline 1 (H2BP1me). Genome-wide analyses revealed an enrichment of H2BP1 methylation at certain transposable elements (TEs) and repetitive genomic sequences. We identified a novel histone methyltransferase, METTL9, which specifically methylates H2BP1. Depletion of METTL9 led to reduced H2BP1me2 levels, an accumulation of gH2A.X, expression activation of some TEs, and increased retrotransposition of a human LINE-1 containing a reporter gene; the latter being a unique feature amongst histone modifiers described to date. These data suggest that reduced H2BP1 methylation may lead to increased TE activity and genome instability. Indeed, decreased levels of H2BP1 methylation in colon tumors correlated with an increase in LINE-1 protein expression. Furthermore, METTL9 depletion in cultured cells led to an enhancement of cellular proliferation, invasion, and migration, suggesting that a loss of H2BP1 methylation could play a role in cancer progression. Thus, we have identified a new role for H2BP1 N-terminal histone methylation in regulating chromatin function and perhaps disease progression, thereby highlighting the role of METTL9 as a novel guardian of genomic stability.

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METTL13 modulates mRNA translation through methylation of eEF1A at Lys55 and the N-terminus, part 2

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