A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA
Research output: Contribution to journal › Journal article › Research › peer-review
Sparsomycin, a broad-spectrum antibiotic, acts at the peptidyl transferase centre of the ribosome, stabilizing peptidyl-tRNA binding at the P-site and weakening ternary complex binding. A sparsomycin-resistant mutant was isolated for the archaeon Halobacterium salinarium and shown to lack a post-transcriptional modification of U2603 (Escherichia coli numbering U2584), which is a universally conserved uridine base located within the peptidyl transferase loop of 23 S rRNA. This mutant also exhibited altered sensitivities to the peptidyl transferase antibiotics anisomycin, chloramphenicol and puromycin. Several lines of evidence indicate that the unmodified uridine base lies within the P-substrate site of the peptidyl transferase centre.
Original language | English |
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Journal | Journal of Molecular Biology |
Volume | 261 |
Issue number | 2 |
Pages (from-to) | 231-238 |
Number of pages | 8 |
ISSN | 0022-2836 |
DOIs | |
Publication status | Published - 16 Aug 1996 |
- 23 S rRNA, Drug-resistant mutant, Peptidyl transferase, Post-transcriptional modification, Sparsomycin
Research areas
ID: 199465012