Jakobsson et al. 2017 (PRJNA380795)
General Details
| Title | Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation |
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| Organism | |
| Number of Samples | 5 |
| Release Date | 2017/03/28 00:00 |
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Study Links
| GWIPS-viz | Trips-Viz |
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| Visit GWIPS-viz | Visit Trips-Viz |
Repository Details
| SRA | SRP102616 |
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| ENA | SRP102616 |
| GEO | |
| BioProject | PRJNA380795 |
Publication
| Title | |
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| Authors | Jakobsson ME,Malecki J,Nilges BS,Moen A,Leidel SA,Falnes PØ |
| Journal | Nucleic acids research |
| Publication Date | 2017 Aug 21 |
| Abstract | Many cellular proteins are methylated on lysine residues and this has been most intensively studied for histone proteins. Lysine methylations on non-histone proteins are also frequent, but in most cases the functional significance of the methylation event, as well as the identity of the responsible lysine (K) specific methyltransferase (KMT), remain unknown. Several recently discovered KMTs belong to the so-called seven-β-strand (7BS) class of MTases and we have here investigated an uncharacterized human 7BS MTase currently annotated as part of the endothelin converting enzyme 2, but which should be considered a separate enzyme. Combining in vitro enzymology and analyzes of knockout cells, we demonstrate that this MTase efficiently methylates K36 in eukaryotic translation elongation factor 1 alpha (eEF1A) in vitro and in vivo. We suggest that this novel KMT is named eEF1A-KMT4 (gene name EEF1AKMT4), in agreement with the recently established nomenclature. Furthermore, by ribosome profiling we show that the absence of K36 methylation affects translation dynamics and changes translation speed of distinct codons. Finally, we show that eEF1A-KMT4 is part of a novel family of human KMTs, defined by a shared sequence motif in the active site and we demonstrate the importance of this motif for catalytic activity. © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. |
| PMC | PMC5737405 |
| PMID | 28520920 |
| DOI |
| Run Accession | Study Accession | Scientific Name | Cell Line | Library Type | Treatment | GWIPS-viz | Trips-Viz | Reads | BAM | BigWig (F) | BigWig (R) | ||
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| SRR5382420 | PRJNA380795 | Homo sapiens | HAP-1 | Ribo-Seq | Cycloheximide |  |
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| SRR5382421 | PRJNA380795 | Homo sapiens | HAP-1 | Ribo-Seq | Cycloheximide | |
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| SRR5382422 | PRJNA380795 | Homo sapiens | HAP-1 | Ribo-Seq | Cycloheximide | |
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| SRR5382423 | PRJNA380795 | Homo sapiens | HEK293 | Ribo-Seq | Cycloheximide | |
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| SRR5382424 | PRJNA380795 | Homo sapiens | HEK293 | Ribo-Seq | Cycloheximide | |
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| Run Accession | Study Accession | Scientific Name | Cell Line | Library Type | Treatment | GWIPS-viz | Trips-Viz | Reads | BAM | BigWig (F) | BigWig (R) |
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