The mitochondrial C-to-U RNA editing factor PPR56 of the moss Physcomitrium patens is an RNA-binding pentatricopeptide repeat protein equipped with a terminal DYW-type cytidine deaminase domain. Transferred into Escherichia coli, PPR56 works faithfully on its two native RNA editing targets, nad3eU230SL and nad4eU272SL, and also converts cytidines into uridines at over 100 off-targets in the bacterial transcriptome. Accordingly, PPR56 is attractive for detailed mechanistic studies in the heterologous bacterial setup, allowing for scoring differential RNA editing activities of many target and protein variants in reasonable time.
View Article and Find Full Text PDFOral biofilms are a prominent cause of a wide variety of oral infectious diseases which are still considered as growing public health problems worldwide. Oral biofilms harbor specific virulence factors that would aggravate the infectious process and present resistance to some traditional therapies. Antimicrobial photodynamic therapy (aPDT) has been proposed as a potential approach to eliminate oral biofilms via -generated reactive oxygen species.
View Article and Find Full Text PDFIn this work, the inclusion complexes of hydrophobic herbicide bensulfuron-methyl (BSM) with β-cyclodextrin (β-CD) and (2-hydroxypropyl)-β-CD (2-HP-β-CD) were prepared and characterized. Phase solubility study showed that both β-CD and 2-HP-β-CD increased the solubility of BSM. Three-dimensional structures of the inclusion complexes were simulated by the molecular docking method.
View Article and Find Full Text PDFA water-soluble inclusion complex for butachlor was prepared by complexation with (2-hydroxypropyl)-β-cyclodextrin (HP-β-CD). Phase solubility results indicated a 1:1 stoichiometric ratio with an apparent stability constant of 864.3 M in the obtained solid complex.
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