Abstract
Long-range interactions involving the P5.1 hairpin of Bacillus RNase P RNA are thought to form a structural truss to support RNA folding and activity. We determined the structure of this element by NMR and refined the structure using residual dipolar couplings from a sample weakly oriented in a dilute liquid crystalline mixture of polyethylene glycol and hexanol. Dipolar coupling refinement improved the global precision of the structure from 1.5 to 1.2 Å (to the mean), revised the bend angle between segments of the P5.1 stem and corroborated the structure of the loop region. The UGAGAU hexaloop of P5.1 contains two stacks of bases on opposite sides of the loop, distinguishing it from GNRA tetraloops. The unusual conformation of the juxtaposed uracil residues within the hexaloop may explain their requirement in transactivation assays.
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Acknowledgements
This work was supported by the Univ. of Missouri Research Board (S.R.V.), NASA (F.J.S.), University of Missouri Molecular Biology Program pre-doctoral fellowship (T.C.L.) and the Missouri Agricultural Experiment Station. The 500 and 600 MHz spectrometers were purchased in part with grants from the National Science Foundation and Univeristy of Missouri Research Board.
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Leeper, T., Martin, M., Kim, H. et al. Structure of the UGAGAU hexaloop that braces Bacillus RNase P for action. Nat Struct Mol Biol 9, 397–403 (2002). https://doi.org/10.1038/nsb775
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DOI: https://doi.org/10.1038/nsb775