Eukaryotic elongation factor 2 can bind to the synthetic oligoribonucleotide that mimics sarcin/ricin domain of rat 28S ribosomal RNA.
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.
Tang
S
S
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.
He
W J
WJ
Xu
H
H
Liu
W Y
WY
Ruan
K C
KC
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000818:Animals; D006153:Guanosine Diphosphate / Q000494:pharmacology; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D008099:Liver / Q000737:chemistry; D009690:Nucleic Acid Conformation; D009843:Oligoribonucleotides / Q000378:metabolism*; D020652:Peptide Elongation Factor 2 / Q000737:chemistry / Q000378:metabolism*; D011189:Potassium Chloride / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012339:RNA, Ribosomal, 28S / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D051381:Rats
D009843:Oligoribonucleotides; D020652:Peptide Elongation Factor 2; D012339:RNA, Ribosomal, 28S; D016601:RNA-Binding Proteins; D006153:Guanosine Diphosphate; D000246:Adenosine Diphosphate Ribose; D006165:Guanylyl Imidodiphosphate; D011189:Potassium Chloride