Abstract
Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction
Highlights
Translation elongation factor eEF1A*GTP carries aminoacyl-tRNA to the A-site of the 80S ribosome facilitating the process of ribosomal protein synthesis
To investigate the role of methylation of several specific Lys residues in eEF1A2 we produced the mutant proteins where these residues were replaced by Arg
“Full” mutant (FM) was produced, in which all five indicated Lys residues were replaced by Arg
Summary
ISSN 1993-6842 (on-line); ISSN 0233-7657 (print) Biopolymers and Cell. Methylation of human elongation factor eEF1A2 is not essential for eEF1A2-eEF1B interaction. Aim. Study on a possible role of methylation of lysine residues of еЕF1А2 in its interactions with the elongation translation complex eEF1B. Mutagenesis, cloning, 293 human cell culture, BRET (bioluminescence resonance energy transfer), cell transfection, HaloTag pull down of protein complexes, Western blot, densitometry. Five mutants of eEF1A2 with a single substitution of methylable lysine residue for arginine and the mutant with all five lysine residues mutated were generated. BRET analysis and HaloTag pull down experiments of isolated protein complexes have shown no differences in interactions of eEF1B subunits with eEF1A2 and its unmethylable mutants. Methylation of eEF1A2 apparently does not influence the interactions of eEF1A2 with eEF1B subunits
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
