Heindl, Hans, Greenwell, Pamela, Weingarten, Noam, Kiss, Tamas, Terstyanszky, Gabor and Weinzierl, Robert O.J. (2011) Cation-? interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain. Biochemical Society Transactions, 39 (1). pp. 31-35. ISSN 0300-5127Full text not available from this repository.
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-? interactions and involve amino acid side chains that are exceptionally highly conserved in all prokaryotic and eukaryotic species.
|Subjects:||University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)
University of Westminster > Science and Technology > Electronics and Computer Science, School of (No longer in use)
|Depositing User:||Miss Nina Watts|
|Date Deposited:||28 Jan 2011 09:44|
|Last Modified:||28 Jan 2011 09:44|
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