TAILIEUCHUNG - Báo cáo khoa hoc : Tertiary interactions between helices h13 and h44 in 16S RNA contribute to the fidelity of translation

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). | IFEBS Journal Tertiary interactions between helices h13 and h44 in 16S RNA contribute to the fidelity of translation Diem K. Tran1 Jason Finley1 Anton Vila-Sanjurjo2 Ajit Lale1 Qing Sun1 and Michael O Connor1 1 Schoolof BiologicalSciences University of Missouri-Kansas City USA 2 Departamento de Quimica Fundamental Universidade da Coruna UDC Spain Keywords A-minor decoding mutagenesis ribosome rRNA Correspondence M. O Connor Schoolof BiologicalSciences University of Missouri-Kansas City 5007 RockhillRoad Kansas City MO 64110 USA Fax 1 816 235 5595 Tel 1 816 235 6372 E-mail oconnormi@ Received 13 June 2011 revised 11 September 2011 accepted 14 September 2011 doi 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. Introduction High-resolution structural analyses of large RNAs and RNPs such as the ribosome have permitted an evaluation of the RNA-RNA and RNA-protein interactions that are important for folding packing stability and function of large RNA molecules 1 2

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