PMID:15003445
| Citation |
Chan, YL, Correll, CC and Wool, IG (2004) The location and the significance of a cross-link between the sarcin/ricin domain of ribosomal RNA and the elongation factor-G. J. Mol. Biol. 337:263-72 |
|---|---|
| Abstract |
During translocation peptidyl-tRNA moves from the A-site to the P-site and mRNA is displaced by three nucleotides in the 3' direction. This reaction is catalyzed by elongation factor-G (EF-G) and is associated with ribosome-dependent hydrolysis of GTP. The molecular basis of translocation is the most important unsolved problem with respect to ribosome function. A critical question, one that might provide a clue to the mechanism of translocation, is the precise identity of the contacts between EF-G and ribosome components. To make the identification, a covalent bond was formed, by ultraviolet irradiation, between EF-G and a sarcin/ricin domain (SRD) oligoribonucleotide containing 5-iodouridine. The cross-link was established, by mass spectroscopy and by Edman degradation, to be between a tryptophan at position 127 in the G domain in EF-G and either one of two 5-iodouridine nucleotides in the sequence UAG2655U in the SRD. G2655 is a critical identity element for the recognition of the factor's ribosomal binding site. The site of the cross-link provides the first direct evidence that the SRD is in close proximity to the EF-G catalytic center. The proximity suggests that the SRD RNA has a role in the activation of GTP hydrolysis that leads to a transition in the conformation of the factor and to its release from the ribosome. |
| Links |
PubMed Online version:10.1016/j.jmb.2004.01.020 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites/genetics; Cross-Linking Reagents; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Peptide Elongation Factor G/chemistry; Peptide Elongation Factor G/metabolism; RNA, Bacterial/chemistry; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Ribosomal/chemistry; RNA, Ribosomal/genetics; RNA, Ribosomal/metabolism; Ricin/chemistry; Ricin/metabolism; Sequence Homology, Amino Acid; Thermus thermophilus/genetics; Thermus thermophilus/metabolism; Ultraviolet Rays |
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