[No authors listed]
Analysis of the Haloarcula marismortui large ribosomal subunit has revealed a common RNA structure that we call the kink-turn, or K-turn. The six K-turns in H.marismortui 23S rRNA superimpose with an r.m.s.d. of 1.7 A. There are two K-turns in the structure of Thermus thermophilus 16S rRNA, and the structures of U4 snRNA and L30e mRNA fragments form K-turns. The structure has a kink in the phosphodiester backbone that causes a sharp turn in the RNA helix. Its asymmetric internal loop is flanked by C-G base pairs on one side and sheared G-A base pairs on the other, with an A-minor interaction between these two helical stems. A derived consensus secondary structure for the K-turn includes 10 consensus nucleotides out of 15, and predicts its presence in the 5'-UTR of L10 mRNA, helix 78 in Escherichia coli 23S rRNA and human RNase MRP. Five K-turns in 23S rRNA interact with nine proteins. While the observed K-turns interact with proteins of unrelated structures in different ways, they interact with L7Ae and two homologous proteins in the same way.
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RR_RS11120, RR_RS11095, rpl19e, RR_RS11105, RR_RS17815, RR_RS11135, RR_RS11165, RR_RS11200, RR_RS11150, rpl4lp, RR_RS11475, RR_RS11190, RR_RS10280, rpl2p, RR_RS11145, RR_RS11175, RR_RS11115, RR_RS11090, RR_RS13190, rpl44e, RR_RS05195, RR_RS04495, rpl7ae, RR_RS14520, RR_RS04320, RR_RS04315, RR_RS17810, rrlH, rrlG, rrlD, rrlC, rrlB, rrlE
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