Abstract
The kink turn is a widespread RNA motif that introduces an acute kink into the axis of duplex RNA, typically comprising a bulge followed by a G.A and A.G pairs. The kinked conformation is stabilized by metal ions, or the binding of proteins including L7Ae. We now demonstrate a third mechanism for the stabilization of k-turn structure, involving tertiary interactions within a larger RNA structure. The SAM-I riboswitch contains an essential standard k-turn sequence that kinks a helix so that its terminal loop can make a long-range interaction. We find that some sequence variations in the k-turn within the riboswitch do not prevent SAM binding, despite preventing the folding of the k-turn in isolation. Furthermore, two crystal structures show that the sequence-variant k-turns are conventionally folded within the riboswitch. This study shows that the folded structure of the k-turn can be stabilized by tertiary interactions within a larger RNA structure.
Original language | English |
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Pages (from-to) | 1233-1240 |
Number of pages | 8 |
Journal | Structure |
Volume | 19 |
Issue number | 9 |
DOIs | |
Publication status | Published - 7 Sept 2011 |
Keywords
- SMALL NUCLEOLAR RNAS
- U4 SNRNA
- S-ADENOSYLMETHIONINE
- PRERIBOSOMAL RNA
- I RIBOSWITCH
- L7AE PROTEIN
- MOTIF
- BINDING
- SITE
- C/D