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    Biochemistry

    Rewiring bacterial two-component systems by modular DNA-binding domain swapping

    Nature Chemical Biology, Published online: 20 May 2019; doi:10.1038/s41589-019-0286-6

    Rewiring of bacterial two-component systems (TCSs) was achieved by DNA-binding domain swapping of the two largest response regulator families, which enables cross-species porting and provides a tool for identifying ligands for uncharacterized TCSs. …read more

    Source:: Nature Biochemistry

          

    Small-molecule control of antibody N-glycosylation in engineered mammalian cells

    Nature Chemical Biology, Published online: 20 May 2019; doi:10.1038/s41589-019-0288-4

    Synthetic gene circuits regulated by small molecules have been used to fine-tune glycosyltransferase expression in CHO cells, providing a method to produce therapeutic monoclonal antibodies with precise glycosylation states. …read more

    Source:: Nature Biochemistry

          

    Covalent binding of uracil DNA glycosylase UdgX to abasic DNA upon uracil excision

    Nature Chemical Biology, Published online: 17 May 2019; doi:10.1038/s41589-019-0289-3

    Structural analysis of uracil DNA glycosylases in complex with DNA reveals that conserved H109 acts as a nucleophile to attack the oxocarbenium ion and makes a covalent bond to the abasic site after uracil excision to form a stable intermediate. …read more

    Source:: Nature Biochemistry

          

    Natural fumigation as a mechanism for volatile transport between flower organs

    Nature Chemical Biology, Published online: 17 May 2019; doi:10.1038/s41589-019-0287-5

    Bioactive sesquiterpenes accumulating in petunia stigmas are synthesized in the floral tube and then transported to the pistil via natural fumigation within the internal airspace of the developing flower. …read more

    Source:: Nature Biochemistry

          

    Suicide inactivation of the uracil DNA glycosylase UdgX by covalent complex formation

    Nature Chemical Biology, Published online: 17 May 2019; doi:10.1038/s41589-019-0290-x

    Structural analysis of uracil DNA glycosylase reveals that its high affinity with DNA substrates derives from a stable intermediate that is formed by conservative H109 in a protruding loop covalently binding to the abasic site after uracil is excised. …read more

    Source:: Nature Biochemistry

          

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