Title | Cation-π interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain |
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Authors | Heindl, H., Greenwell, P., Weingarten, N., Kiss, T., Terstyanszky, G. and Weinzierl, R.O.J. |
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Abstract | RNAPs (RNA polymerases) are complex molecular machines that contain a highly conserved catalytic site surrounded by conformationally flexible domains. High-throughput mutagenesis in the archaeal model system Methanocaldococcus jannaschii has demonstrated that the nanomechanical properties of one of these domains, the bridge-helix, exert a key regulatory role on the rate of the NAC (nucleotide-addition cycle). Mutations that increase the probability and/or half-life of kink formation in the BH-HC (bridge-helix C-terminal hinge) cause a substantial increase in specific activity ('superactivity'). Fully atomistic molecular dynamics simulations show that kinking of the BH-HC appears to be driven by cation-π interactions and involve amino acid side chains that are exceptionally highly conserved in all prokaryotic and eukaryotic species. |
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Journal | Biochemical Society Transactions |
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Journal citation | 39 (1), pp. 31-35 |
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ISSN | 0300-5127 |
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Year | Feb 2011 |
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Publisher | Portland Press |
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Digital Object Identifier (DOI) | https://doi.org/10.1042/BST0390031 |
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Publication dates |
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Published | Feb 2011 |
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