A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA
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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; Ureña, Dionisio; Garrett, Roger A.; Ballesta, Juan P.G.
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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TY - JOUR
T1 - A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA
AU - Lázaro, Ester
AU - Rodriguez-Fonseca, Cristina
AU - Porse, Bo
AU - Ureña, Dionisio
AU - Garrett, Roger A.
AU - Ballesta, Juan P.G.
PY - 1996/8/16
Y1 - 1996/8/16
N2 - 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.
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.
KW - 23 S rRNA
KW - Drug-resistant mutant
KW - Peptidyl transferase
KW - Post-transcriptional modification
KW - Sparsomycin
UR - http://www.scopus.com/inward/record.url?scp=0030590237&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1996.0455
DO - 10.1006/jmbi.1996.0455
M3 - Journal article
C2 - 8757290
AN - SCOPUS:0030590237
VL - 261
SP - 231
EP - 238
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 2
ER -
ID: 199465012