Journal
RNA
Volume 16, Issue 12, Pages 2319-2324Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.2357210
Keywords
ribosome; rRNA modification; RNA structure; Thermus; decoding; antibiotic resistance
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Funding
- National Institutes of Health [GM19756, GM19756-37S1]
- MRC [MC_U105184332] Funding Source: UKRI
- Medical Research Council [MC_U105184332] Funding Source: researchfish
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All organisms incorporate post-transcriptional modifications into ribosomal RNA, influencing ribosome assembly and function in ways that are poorly understood. The most highly conserved modification is the dimethylation of two adenosines near the 39 end of the small subunit rRNA. Lack of these methylations due to deficiency in the KsgA methyltransferase stimulates translational errors during both the initiation and elongation phases of protein synthesis and confers resistance to the antibiotic kasugamycin. Here, we present the X-ray crystal structure of the Thermus thermophilus 30S ribosomal subunit lacking these dimethylations. Our data indicate that the KsgA-directed methylations facilitate structural rearrangements in order to establish a functionally optimum subunit conformation during the final stages of ribosome assembly.
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