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TitleMETTL18-mediated histidine methylation of RPL3 modulates translation elongation for proteostasis maintenance.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateJun 8, 2022
AuthorsEriko Matsuura-Suzuki / Tadahiro Shimazu / Mari Takahashi / Kaoru Kotoshiba / Takehiro Suzuki / Kazuhiro Kashiwagi / Yoshihiro Sohtome / Mai Akakabe / Mikiko Sodeoka / Naoshi Dohmae / Takuhiro Ito / Yoichi Shinkai / Shintaro Iwasaki /
PubMed AbstractProtein methylation occurs predominantly on lysine and arginine residues, but histidine also serves as a methylation substrate. However, a limited number of enzymes responsible for this modification ...Protein methylation occurs predominantly on lysine and arginine residues, but histidine also serves as a methylation substrate. However, a limited number of enzymes responsible for this modification have been reported. Moreover, the biological role of histidine methylation has remained poorly understood to date. Here, we report that human METTL18 is a histidine methyltransferase for the ribosomal protein RPL3 and that the modification specifically slows ribosome traversal on Tyr codons, allowing the proper folding of synthesized proteins. By performing an in vitro methylation assay with a methyl donor analog and quantitative mass spectrometry, we found that His245 of RPL3 is methylated at the τ- position by METTL18. Structural comparison of the modified and unmodified ribosomes showed stoichiometric modification and suggested a role in translation reactions. Indeed, genome-wide ribosome profiling and an in vitro translation assay revealed that translation elongation at Tyr codons was suppressed by RPL3 methylation. Because the slower elongation provides enough time for nascent protein folding, RPL3 methylation protects cells from the cellular aggregation of Tyr-rich proteins. Our results reveal histidine methylation as an example of a ribosome modification that ensures proteome integrity in cells.
External linksElife / PubMed:35674491 / PubMed Central
MethodsEM (single particle)
Resolution2.72 Å
Structure data

31465

7f5s

EMDB-31465, PDB-7f5s:
human delta-METTL18 60S ribosome
Method: EM (single particle) / Resolution: 2.72 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • Human (human)
KeywordsRIBOSOME / 60S

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