Summary of 277-Matsuura-Suzuki-CryoEM

SSBD:database
SSBD:database URL
Title
Cryo-electron microscopy (cryo-EM) microscopy images of human ribosomes isolated from METTL18 KO cells.
Description
-
Relase date
2023-08-30
Updated date
-
License
CC BY
Kind
Image data based on Experiment
Number of Datasets
2 ( Image datasets: 2, Quantitative data datasets: 0 )
Size of Datasets
1.1 TB ( Image datasets: 1.1 TB, Quantitative data datasets: 0 bytes )

Organism(s)
Homo sapiens
Cell lines(s)
METTL18 KO cell
Gene symbol(s)
NA
Protein name(s)
NA

Datatype
-
Molecular Function (MF)
Biological Process (BP)
Cellular Component (CC)
ribosome
Biological Imaging Method
cryo-electron microscopy
T scale
-

Image Acquisition
Experiment type
-
Microscope type
-
Acquisition mode
-
Contrast method
-
Microscope model
-
Detector model
-
Objective model
-
Filter set
-

Related paper(s)

Eriko 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 (2022) METTL18-mediated histidine methylation of RPL3 modulates translation elongation for proteostasis maintenance., eLife, Volume 11

Published in 2022 Jun 8 (Electronic publication in June 8, 2022, midnight )

(Abstract) 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 tau-N 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.
(MeSH Terms)

Contact
Tadahiro Shimazu, Takuhiro Ito, Yoichi Shinkai, Shintaro Iwasaki , RIKEN, RIKEN, RIKEN, RIKEN , RIKEN Cluster for Pioneering Research, RIKEN Center for Biosystems Dynamics Research, RIKEN Cluster for Pioneering Research, RIKEN Cluster for Pioneering Research , Cellular Memory Laboratory , Laboratory for Translation Structural Biology, Cellular Memory Laboratory , RNA Systems Biochemistry Laboratory
Contributors


Dataset List of 277-Matsuura-Suzuki-CryoEM

#
Dataset ID
Kind
Size
4D View
SSBD:OMERO
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# 10986
Dataset Kind Image data
Dataset Size 581.2 GB
4D view
SSBD:OMERO
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# 10987
Dataset Kind Image data
Dataset Size 511.6 GB
4D view
SSBD:OMERO
Download BDML
Download Image data