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
Organism
Number of Samples 5
Release Date 2017/03/28 00:00
Sequencing Types
Protocol Details

Study Links

Repository Details

SRA SRP102616
ENA SRP102616
GEO GSE97140
BioProject PRJNA380795

Publication

Title
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)
SRR5382420 PRJNA380795 Homo sapiens HAP-1 Ribo-Seq Cycloheximide
SRR5382421 PRJNA380795 Homo sapiens HAP-1 Ribo-Seq Cycloheximide
SRR5382422 PRJNA380795 Homo sapiens HAP-1 Ribo-Seq Cycloheximide
SRR5382423 PRJNA380795 Homo sapiens HEK293 Ribo-Seq Cycloheximide
SRR5382424 PRJNA380795 Homo sapiens HEK293 Ribo-Seq Cycloheximide
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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