Human eukaryotic elongation factor 1A forms oligomers through specific cysteine residues

Eukaryotic elongation factor 1A （eEF1A） is a multifunctional protein involved in bundling actin, sever- ing microtubule, activating the phosphoinositol-4 kinase, and recruiting aminoacyl-tRNAs to ribo- somes during protein biosynthesis. Although evidence has shown the presence of the isoform eEFIA1...

Full description

Saved in:
Bibliographic Details
Published in:Acta biochimica et biophysica Sinica 2015-12, Vol.47 (12), p.1011-1017
Main Authors: Liu, Tao, Yang, Yu, Wang, Di, Xiao, Yan, Du, Guangshi, Wu, Lei, Ding, Muran, Li, Ling, Wu, Chuanfang
Format: Article
Language:English
Subjects:
Actins - chemistry
Cysteine - chemistry
HEK293 Cells
Humans
Hydrogen Peroxide - chemistry
Mutagenesis
Mutation
Open Reading Frames
Oxidative Stress
Peptide Elongation Factor 1 - chemistry
Phosphorylation
Protein Binding
Protein Biosynthesis
Protein Isoforms - chemistry
Recombinant Proteins - chemistry
Sequence Homology, Amino Acid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Eukaryotic elongation factor 1A （eEF1A） is a multifunctional protein involved in bundling actin, sever- ing microtubule, activating the phosphoinositol-4 kinase, and recruiting aminoacyl-tRNAs to ribo- somes during protein biosynthesis. Although evidence has shown the presence of the isoform eEFIA1 oligomers, the substantial mechanism of the self-association remains unclear. Herein, we found that human eEF1A1 could spontaneously form oligomers. Specifically, mutagenes!s screen on cysteine residues demonstrated that CysTM was essential for eEFIA1 oligomerization. In addition, we also found that hydrogen peroxide treatment could induce the formation of eEFIA oligomers in cells. By cysteine replacement, eEF1A2 isoform displayed the ability to oligomerize in cells under the oxidative environment. In summary, in this study we characterized eEFIA1 oligomerization and demonstrated that specific cysteine residues are required for this oligomerization activity.
ISSN:1672-9145
1745-7270
DOI:10.1093/abbs/gmv113