Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 379, Issue 3, Pages 505-519Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.03.075
Keywords
antibiotic resistance; large ribosomal subunit; 23S rRNA mutation; X-ray crystal structure; Haloarcula marismortui
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Funding
- NIGMS NIH HHS [P01 GM022778-300008, P01 GM022778-29, P01 GM022778-290008, P01 GM022778-30, P01GM022778, F32 GM067354, F32-GM067354, P01 GM022778] Funding Source: Medline
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Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome. (c) 2008 Elsevier Ltd. All rights reserved.
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