SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis.
Amino Acid Sequence
HEK293 Cells
Histone-Lysine N-Methyltransferase
/ antagonists & inhibitors
Humans
Lysine
/ chemistry
Methylation
Protein Biosynthesis
Protein Domains
Protein Interaction Domains and Motifs
Protein Subunits
/ chemistry
RNA Interference
RNA, Small Interfering
/ metabolism
Ribosomal Proteins
/ chemistry
Two-Hybrid System Techniques
Lysine methylation
Protein-protein interaction
RPL36A
SETD7
Translation
Journal
Biochimica et biophysica acta. Molecular cell research
ISSN: 1879-2596
Titre abrégé: Biochim Biophys Acta Mol Cell Res
Pays: Netherlands
ID NLM: 101731731
Informations de publication
Date de publication:
02 2020
02 2020
Historique:
received:
24
07
2019
revised:
21
10
2019
accepted:
13
11
2019
pubmed:
22
11
2019
medline:
21
4
2020
entrez:
22
11
2019
Statut:
ppublish
Résumé
Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9-mediated methylation often regulates the stability, sub-cellular localization and protein-protein interactions of its substrate proteins. Here, we aimed to identify novel biological processes regulated by SET7/9 by identifying new interaction partners. For this we used yeast two-hybrid screening and identified the large subunit ribosomal protein, eL42 as a potential interactor of SET7/9. We confirmed the SET7/9-eL42 interaction by co-immunoprecipitation and GST pulldown studies. The N-terminal MORN domain of SET7/9 is essential for its interaction with eL42. Importantly, we identified that SET7/9 methylates eL42 at three different lysines - Lys53, Lys80 and Lys100 through site-directed mutagenesis. By puromycin incorporation assay, we find that SET7/9-mediated methylation of eL42 affects global translation. This study identifies a new role of the functionally versatile SET7/9 lysine methyltransferase in the regulation of global protein synthesis.
Identifiants
pubmed: 31751593
pii: S0167-4889(19)30219-8
doi: 10.1016/j.bbamcr.2019.118611
pii:
doi:
Substances chimiques
Protein Subunits
0
RNA, Small Interfering
0
RPL36A protein, human
0
Ribosomal Proteins
0
Histone-Lysine N-Methyltransferase
EC 2.1.1.43
SETD7 protein, human
EC 2.1.1.43
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
118611Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.