WGS histidine overproducers
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB45772 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR6087160_1.fastq.gz | Fastqsanger.gz | |||
| ERR6087160_2.fastq.gz | Fastqsanger.gz | |||
| ERR6087161_1.fastq.gz | Fastqsanger.gz | |||
| ERR6087161_2.fastq.gz | Fastqsanger.gz | |||
| ERR6087162_1.fastq.gz | Fastqsanger.gz |
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2023-03-10 | PXD034865 | Pride
Project description:Protein methylation occurs predominantly on lysine and arginine residues, but histidine also serves as a substrate for the modification. However, a limited number of enzymes responsible for this modification have been reported. Moreover, the biological role of histidine methylation has remained poorly understood. Here, we report that human METTL18 is a histidine methyltransferase for the ribosomal protein RPL3 and that the modification specifically slows ribosome traverse on tyrosine 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-N position by METTL18. Structural comparison of the modified and unmodified ribosomes showed stoichiometric modification and suggested a role in translation tuning. Indeed, genome-wide ribosome profiling revealed suppressed ribosomal translocation at tyrosine codons 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 code” that ensures proteome integrity in cells.
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Project description:For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.
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