PMID:11583158
| Citation |
Zwieb, C, Guven, SA, Wower, IK and Wower, J (2001) Three-dimensional folding of the tRNA-like domain of Escherichia coli tmRNA. Biochemistry 40:9587-95 |
|---|---|
| Abstract |
UV irradiation of Escherichia coli tmRNA both on and off the ribosome induced covalent cross-links between its 3'- and its 5'-terminal segments. Cross-linking was unaffected in a molecule that lacked the tag-peptide codon region and pseudoknots 2, 3, and 4. Intact and truncated cross-linked tmRNAs were aminoacylated as efficiently as the respective nonirradiated molecules, suggesting that the added UV-induced bonds did not disturb tmRNA conformation. Using RNase H digestion followed by primer extension with reverse transcriptase, two cross-linked sites were identified within the tRNA-like region of tmRNA. The first was formed between nucleotides U9/U10 near the 5' end and nucleotides C346/U347 in the T loop. The second cross-link involved residues at positions 25-28 and 326-329 within helix 2a. Together with comparative sequence analysis, these findings yielded a three-dimensional model of the tRNA-like domain of E. coli tmRNA. Despite significant reduction of the D domain and the proximity of U9/U10 and C346/U347, the model closely resembles the L-shaped structure of canonical tRNA. |
| Links | |
| Keywords |
Base Sequence; Cross-Linking Reagents; Escherichia coli/chemistry; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Folding; Protein Structure, Tertiary; RNA, Bacterial/chemistry; RNA, Bacterial/radiation effects; RNA, Transfer/chemistry; RNA, Transfer/radiation effects; Ultraviolet Rays |
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