Three-dimensional folding of the tRNA-like domain of escherichia coli tmRNA

C. Zwieb, S. A. Guven, I. K. Wower, J. Wower

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)9587-9595
Number of pages9
JournalBiochemistry
Volume40
Issue number32
DOIs
StatePublished - Aug 14 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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