Eukaryotic elongation factor 2 can bind to the synthetic oligoribonucleotide that mimics sarcin/ricin domain of rat 28S ribosomal RNA

• Published in: Molecular and cellular biochemistry 2001-07, Vol.223 (1-2), p.117-121
• Main Authors: Tang, S, He, W J, Xu, H, Liu, W Y, Ruan, K C
• Format: Article
• Language: English
• Subjects: Adenosine diphosphate; Adenosine Diphosphate Ribose - metabolism; Amino acids; Animals; Biosynthesis; Cellular biology; Eukaryotes; Guanosine Diphosphate - pharmacology; Guanylyl Imidodiphosphate - pharmacology; Liver - chemistry; Nucleic Acid Conformation; Oligoribonucleotides - metabolism; Peptide Elongation Factor 2 - chemistry; Peptide Elongation Factor 2 - metabolism; Potassium Chloride - chemistry; Protein Binding; Protein Structure, Tertiary; Protein synthesis; Proteins; Rats; RNA, Ribosomal, 28S - chemistry; RNA, Ribosomal, 28S - metabolism; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; Toxins; Translocation
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1023/A:1017914413081

Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to P site by binding to the ribosome. In this work, the complex formation of rat liver eEF2 with a synthetic oligoribonucleotide (SRD RNA) that mimics sarcin/ricin domain of rat 28S ribosomal RNA is invested in vitro. Purified eEF2 can specifically bind SRD RNA to form a stable complex. tRNA competes with SRD RNA in binding to eEF2 in a less extent. Pretreatment of eEF2 with GDP or ADP-ribosylation of eEF2 by diphtheria toxin can obviously reduce the ability of eEF2 to form the complex with the synthetic oligoribonucleotide. These results indicate that eEF2 is likely to bind directly to the sarcin/ricin domain of 28S ribosomal RNA in the process of protein synthesis.