PMID:9356440
| Citation |
Munishkin, A and Wool, IG (1997) The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA. Proc. Natl. Acad. Sci. U.S.A. 94:12280-4 |
|---|---|
| Abstract |
An oligoribonucleotide (a 27-mer) that mimics the sarcin/ricin (S/R) domain of Escherichia coli 23S rRNA binds elongation factor EF-G; the Kd is 6.9 microM, whereas for binding to ribosomes it is 0.7 microM. Binding saturates when EF-G and the S/R RNA are equimolar; at saturation 70% of the input RNA is in complexes with EF-G. Binding of EF-G to S/R RNA does not require GTP but is inhibited by GDP; the inhibition by GDP is overcome by GTP. The effects of mutations of the S/R domain nucleotides G2655, A2660, and G2661 suggest that EF-G recognizes the conformation of the RNA rather than the identity of the nucleotides. EF-G also binds to an oligoribonucleotide (an 84-mer) that has the thiostrepton region of 23S rRNA; however, EF-G binds independently to S/R and thiostrepton oligoribonucleotides. |
| Links | |
| Keywords |
Base Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; Molecular Sequence Data; Oligonucleotides/chemistry; Oligonucleotides/genetics; Oligonucleotides/metabolism; Peptide Elongation Factor G; Peptide Elongation Factors/metabolism; Protein Binding; RNA, Ribosomal, 23S/chemistry; RNA, Ribosomal, 23S/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/metabolism; Ribosomes/chemistry; Ribosomes/genetics; Ribosomes/metabolism; Ricin/chemistry; Thiostrepton/chemistry; Thiostrepton/metabolism |
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