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Tertiary interactions between helices h13 and h44 in 16S RNA contribute to the fidelity of translation
Author(s) -
Tran Diem K.,
Finley Jason,
VilaSanjurjo Antón,
Lale Ajit,
Sun Qing,
O’Connor Michael
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08363.x
Subject(s) - transfer rna , protein subunit , helix (gastropod) , biology , ribosomal rna , mutant , 30s , translation (biology) , mutagenesis , nucleotide , ribosome , proofreading , base pair , genetics , computational biology , rna , dna , polymerase , gene , ecology , snail , messenger rna
The A‐minor interaction, formed between single‐stranded adenosines and the minor groove of a receptor helix, is among the most common motifs found in rRNA. Among the A‐minors found in 16S rRNA are a set of interactions between adenosines at positions 1433, 1434 and 1468 in helix 44 (h44) and their receptors in the nucleotide 320–340 region of helix 13 (h13). These interactions have been implicated in the maintenance of translational accuracy, because base substitutions at the adjacent C1469 increase miscoding errors. We have tested their functional significance through mutagenesis of h13 and h44. Mutations at the h44 A residues, or the A‐minor receptors in h13, increase a variety of translational errors and a subset of the mutants show decreased association between 30S and 50S ribosomal subunits. These results are consistent with the involvement of h13–h44 interactions in the alignment and packing of these helices in the 30S subunit and the importance of this helical alignment for tRNA selection and subunit–subunit interaction.