Translation elongation factor eEF1A1 is a novel partner of a multifunctional protein Sgt1

Oleksandra Novosylna; Ewelina Jurewicz; Nikolay Pydiura; Agnieszka Goral; Anna Filipek; Boris Negrutskii; Anna El'skaya

doi:10.1016/j.biochi.2015.10.026

Translation elongation factor eEF1A1 is a novel partner of a multifunctional protein Sgt1

Biochimie. 2015 Dec:119:137-45. doi: 10.1016/j.biochi.2015.10.026. Epub 2015 Nov 9.

Authors

Oleksandra Novosylna¹, Ewelina Jurewicz², Nikolay Pydiura³, Agnieszka Goral², Anna Filipek⁴, Boris Negrutskii⁵, Anna El'skaya¹

Affiliations

¹ State Key Laboratory on Molecular and Cell Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine.
² Nencki Institute of Experimental Biology, 3 Pasteur str., 02-093 Warsaw, Poland.
³ State Key Laboratory on Molecular and Cell Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine; Laboratory of Bioinformatics and Structural Biology, Institute of Food Biotechnology and Genomics, 2A Оsipovskogo str., Kiev 04123, Ukraine.
⁴ Nencki Institute of Experimental Biology, 3 Pasteur str., 02-093 Warsaw, Poland. Electronic address: a.filipek@nencki.gov.pl.
⁵ State Key Laboratory on Molecular and Cell Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine. Electronic address: negrutskii@imbg.org.ua.

PMID: 26545799
DOI: 10.1016/j.biochi.2015.10.026

Abstract

Mammalian translation elongation factor eEF1A is involved in ribosomal polypeptide synthesis. Also, the protein fulfills many additional duties in an eukaryotic cell. Here, we identified a novel partner of the eEF1A1 isoform, namely Sgt1, a protein that possesses co-chaperon properties and participates in antiviral defense processes. By applying different methods, we demonstrated the interaction between eEF1A1 and Sgt1 using both purified proteins and cell lysates. We also found that the D2 and D3 domains of eEF1A1 and the TPR domain of Sgt1 are involved in complex formation. Modeling of the Sgt1-eEF1A1 complex suggested both shape and charge complementarities of the eEF1A1-Sgt1 interface stabilized by a number of salt bridges. As long as such interaction mode is typical more for protein-nucleic acid interaction we suggested a possibility that Sgt1 competes with viral RNA for binding to eEF1A and obtained in vitro evidence to this effect.

Keywords: Protein–protein interaction; Sgt1; eEF1A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding, Competitive
Cell Cycle Proteins / chemistry
Cell Cycle Proteins / genetics
Cell Cycle Proteins / metabolism*
Glutathione Transferase / chemistry
Glutathione Transferase / genetics
Glutathione Transferase / metabolism
HEK293 Cells
Hepatocytes / cytology
Hepatocytes / enzymology
Hepatocytes / metabolism*
Humans
Ligands
Models, Molecular*
Molecular Docking Simulation
Peptide Elongation Factor 1 / chemistry
Peptide Elongation Factor 1 / genetics
Peptide Elongation Factor 1 / isolation & purification
Peptide Elongation Factor 1 / metabolism*
Peptide Fragments
Protein Interaction Domains and Motifs
Protein Isoforms / chemistry
Protein Isoforms / genetics
Protein Isoforms / metabolism
Protein Multimerization
Protein Stability
Protein Structure, Tertiary
RNA, Viral / chemistry
RNA, Viral / metabolism
Rabbits
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / metabolism
Recombinant Proteins / chemistry
Recombinant Proteins / metabolism

Substances

Cell Cycle Proteins
EEF1A1 protein, human
Ligands
Peptide Elongation Factor 1
Peptide Fragments
Protein Isoforms
RNA, Viral
Recombinant Fusion Proteins
Recombinant Proteins
SUGT1 protein, human
Glutathione Transferase