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Mechanistic and Structural Studies of Protein-Only RNase P Compared to Ribonucleoproteins Reveal the Two Faces of the Same Enzymatic Activity
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Biomolecules 2016, 6(3), 38;

Inhibition of Bacterial RNase P RNA by Phenothiazine Derivatives

Department of Cell and Molecular Biology, Box 596, Biomedical Centre, Uppsala SE-751 24, Sweden
Author to whom correspondence should be addressed.
Academic Editor: Denis Drainas
Received: 30 June 2016 / Revised: 24 August 2016 / Accepted: 26 August 2016 / Published: 8 September 2016
(This article belongs to the Special Issue Function and Structure of RNase P in Fungi, Bacteria and Human Cells)
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There is a need to identify novel scaffolds and targets to develop new antibiotics. Methylene blue is a phenothiazine derivative, and it has been shown to possess anti-malarial and anti-trypanosomal activities. Here, we show that different phenothiazine derivatives and pyronine G inhibited the activities of three structurally different bacterial RNase P RNAs (RPRs), including that from Mycobacterium tuberculosis, with Ki values in the lower μM range. Interestingly, three antipsychotic phenothiazines (chlorpromazine, thioridazine, and trifluoperazine), which are known to have antibacterial activities, also inhibited the activity of bacterial RPRs, albeit with higher Ki values than methylene blue. Phenothiazines also affected lead(II)-induced cleavage of bacterial RPR and inhibited yeast tRNAPhe, indicating binding of these drugs to functionally important regions. Collectively, our findings provide the first experimental data showing that long, noncoding RNAs could be targeted by different phenothiazine derivatives. View Full-Text
Keywords: RNA processing; catalytic RNA; RNase P; phenothiazines RNA processing; catalytic RNA; RNase P; phenothiazines

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Wu, S.; Mao, G.; Kirsebom, L.A. Inhibition of Bacterial RNase P RNA by Phenothiazine Derivatives. Biomolecules 2016, 6, 38.

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