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The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

ABSTRACT: Post-translational methylation plays a crucial role in regulating and optimizing protein function. Protein histidine methylation, occurring as the two isomers 1- and 3- methylhistidine (1MH and 3MH), was first reported five decades ago, but remains largely unexplored. Here we report that METTL9 is a broad-specificity methyltransferase (MTase) that mediates the formation of the majority of 1MH present in mouse and human proteomes. The minimal requirement for METTL9-catalyzed methylation is a His-x-His (HxH) motif, where "x" is preferably a small amino acid, allowing METTL9 to methylate a number of HxH-containing proteins. Here, we show that the immunomodulatory protein S100A9 and the NDUFB3 subunit of mitochondrial respiratory Complex I are methylated at HxH motif using MALDI-TOF MS.

INSTRUMENT(S): Bruker Daltonics flex series

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Permanent Cell Line Cell, Cell Culture, Neutrophil

SUBMITTER: Takehiro Suzuki

LAB HEAD: Naoshi Dohmae

PROVIDER: PXD022067 | Pride | 2020-11-23

REPOSITORIES: Pride

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			Action	DRS
	F208125.dat	Other
	F208125.mgf	Mgf
	F208125.mzid.gz	Mzid
	F208127.dat	Other
	F208127.mgf	Mgf

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The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

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