siRNA screening identifies METTL9 as a histidine Nπ-methyltransferase that targets the proinflammatory protein S100A9

Daitoku, Hiroaki; Someya, Momoka; Kako, Koichiro; Hayashi, Takahiro; Tajima, Tatsuya; Haruki, Hikari; Sekiguchi, Naoki; Uetake, Toru; Akimoto, Yuto; Fukamizu, Akiyoshi

doi:10.1016/j.jbc.2021.101230

Cited by 13 publications

(13 citation statements)

References 35 publications

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“…S100A9 was found to carry histidine methylation at the His107 residue in previous mass spectrum data ( Raftery et al, 1996 ). We and other groups have previously reported that METTL9 methylates S100A9 at the His107 residue ( Daitoku et al, 2021 ; Davydova et al, 2021 ; Lv et al, 2021 ). However, whether METTL9-catalyzed His107 methylation of S100A9 has bona fide physiological functions remains unknown.…”

Section: Dear Editormentioning

confidence: 80%

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METTL9-catalyzed histidine methylation of S100A9 suppresses the anti-Staphylococcus aureus activity of neutrophils

Cao

et al. 2023

Protein &Amp; Cell

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Section: Dear Editormentioning

confidence: 80%

“…1K ). Indeed, His107 methylation of an S100A9 peptide (16 amino acids) showed reduced zinc-binding activity ( Daitoku et al, 2021 ).…”

Section: Dear Editormentioning

confidence: 99%

METTL9-catalyzed histidine methylation of S100A9 suppresses the anti-Staphylococcus aureus activity of neutrophils

Cao

et al. 2023

Protein &Amp; Cell

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“…Using tandem "HxH" repeats motif derived from SLC39A7 as a model substrate, we revealed preferred consecutive methylation events catalyzed by METTL9, notably in "C-to-N" direction (Figure 7). Depending on its cognate substrate, METTL9-mediated histidine methylation may regulate many cellular functions, including zinc transport 16 , ER stress 16 , and innate immunity 17 . Functionally, the consecutive and directional catalysis feature of METTL9 may help to determine its substrate preference and regulate corresponding activities (Fig.…”

Section: Discussionmentioning

confidence: 99%

Molecular basis for protein histidine N1-specific methylation of the “His-x-His” motifs by METTL9

Zhao¹,

Zhou²,

Li³

et al. 2023

Cell Insight

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“…This highlights that methylation beyond lysine and arginine is more prevalent than perhaps otherwise considered and should be further investigated in other eukaryotes. In fact, it has recently become apparent that histidine methylation and methyltransferases are prevalent in human ( 58 , 88 – 91 ). Furthermore, it should be considered that methyltransferases in non-model organisms may catalyze these noncanonical forms of methylation, rather than just lysine and arginine methylation.…”

Section: Why the Yeast Protein Methylation Network Is Near-completementioning

confidence: 99%

The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification

Hamey

Wilkins

2023

Proc. Natl. Acad. Sci. U.S.A.

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Defining all sites for a post-translational modification in the cell, and identifying their upstream modifying enzymes, is essential for a complete understanding of a modification’s function. However, the complete mapping of a modification in the proteome and definition of its associated enzyme–substrate network is rarely achieved. Here, we present the protein methylation network for Saccharomyces cerevisiae. Through a formal process of defining and quantifying all potential sources of incompleteness, for both the methylation sites in the proteome and also protein methyltransferases, we prove that this protein methylation network is now near-complete. It contains 33 methylated proteins and 28 methyltransferases, comprising 44 enzyme-substrate relationships, and a predicted further three enzymes. While the precise molecular function of most methylation sites is unknown, and it remains possible that other sites and enzymes remain undiscovered, the completeness of this protein modification network is unprecedented and allows us to holistically explore the role and evolution of protein methylation in the eukaryotic cell. We show that while no single protein methylation event is essential in yeast, the vast majority of methylated proteins are themselves essential, being primarily involved in the core cellular processes of transcription, RNA processing, and translation. This suggests that protein methylation in lower eukaryotes exists to fine-tune proteins whose sequences are evolutionarily constrained, providing an improvement in the efficiency of their cognate processes. The approach described here, for the construction and evaluation of post-translational modification networks and their constituent enzymes and substrates, defines a formal process of utility for other post-translational modifications.

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siRNA screening identifies METTL9 as a histidine Nπ-methyltransferase that targets the proinflammatory protein S100A9

Abstract: A, siRNA screening identifies METTL9 as a histidine N π methyltransferase that targets the pro-inflammatory protein S100A9,

Cited by 13 publications

References 35 publications

METTL9-catalyzed histidine methylation of S100A9 suppresses the anti-Staphylococcus aureus activity of neutrophils

METTL9-catalyzed histidine methylation of S100A9 suppresses the anti-Staphylococcus aureus activity of neutrophils

Molecular basis for protein histidine N1-specific methylation of the “His-x-His” motifs by METTL9

The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification

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