Proteomics

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METTL13 modulates mRNA translation through methylation of eEF1A at Lys55 and the N-terminus

ABSTRACT: The experiment aimed at identifying lysine methylation dependent interactions for eEF1A. FLAG-tagged wild type eEF1A and a methylation deficient mutant, carrying lysine-to-arginine mutations of the well-established methylation sites (Lys36, Lys55, Lys79, Lys165 and Lys318) were overexpressed in HEK-293 cells and co-purifying proteins were quantified using the MaxLFQ algorithm. FLAG-tagged

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Diploid Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Magnus Jakobsson  

LAB HEAD: Jesper Velgard Olsen

PROVIDER: PXD009895 | Pride | 2018-07-04

REPOSITORIES: Pride

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20160914_QE5_nLC11_MJ_wDox_eEF1A1_5KR_rep1.raw Raw
20160914_QE5_nLC11_MJ_wDox_eEF1A1_5KR_rep2.raw Raw
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20160914_QE5_nLC11_MJ_wDox_eEF1A1_5KR_rep4.raw Raw
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Publications

Eukaryotic elongation factor 1 alpha (eEF1A) delivers aminoacyl-tRNA to the ribosome and thereby plays a key role in protein synthesis. Human eEF1A is subject to extensive post-translational methylation, but several of the responsible enzymes remain unknown. Using a wide range of experimental approaches, we here show that human methyltransferase (MTase)-like protein 13 (METTL13) contains two distinct MTase domains targeting the N terminus and Lys55 of eEF1A, respectively. Our biochemical and str  ...[more]

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