A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA

Ester Lázaro; Cristina Rodriguez-Fonseca; Bo Porse; Dionisio Ureña; Roger A. Garrett; Juan P.G. Ballesta

doi:10.1006/jmbi.1996.0455

A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA

Ester Lázaro, Cristina Rodriguez-Fonseca, Bo Porse, Dionisio Ureña, Roger A. Garrett^*, Juan P.G. Ballesta

^*Corresponding author for this work

35 Citations (Scopus)

Abstract

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
Journal	Journal of Molecular Biology
Volume	261
Issue number	2
Pages (from-to)	231-238
Number of pages	8
ISSN	0022-2836
DOIs	https://doi.org/10.1006/jmbi.1996.0455
Publication status	Published - 16 Aug 1996

Keywords

23 S rRNA
Drug-resistant mutant
Peptidyl transferase
Post-transcriptional modification
Sparsomycin

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10.1006/jmbi.1996.0455

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A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA. / Lázaro, Ester; Rodriguez-Fonseca, Cristina; Porse, Bo et al.
In: Journal of Molecular Biology, Vol. 261, No. 2, 16.08.1996, p. 231-238.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "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.",

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AU - Lázaro, Ester

AU - Rodriguez-Fonseca, Cristina

AU - Porse, Bo

AU - Ureña, Dionisio

AU - Garrett, Roger A.

AU - Ballesta, Juan P.G.

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AB - 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.

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KW - Peptidyl transferase

KW - Post-transcriptional modification

KW - Sparsomycin

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A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA

Abstract

Keywords

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