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• W2516230003 endingPage "gkw740" @default.
• W2516230003 startingPage "gkw740" @default.
• W2516230003 abstract "The topological state of DNA is important for replication, recombination and transcription, and is regulated in vivo by DNA topoisomerases. Gyrase introduces negative supercoils into DNA at the expense of ATP hydrolysis. It is the accepted view that gyrase achieves supercoiling by a strand passage mechanism, in which double-stranded DNA is cleaved, and a second double-stranded segment is passed through the gap, converting a positive DNA node into a negative node. We show here that gyrase with only one catalytic tyrosine that cleaves a single strand of its DNA substrate can catalyze DNA supercoiling without strand passage. We propose an alternative mechanism for DNA supercoiling via nicking and closing of DNA that involves trapping, segregation and relaxation of two positive supercoils. In contrast to DNA supercoiling, ATP-dependent relaxation and decatenation of DNA by gyrase lacking the C-terminal domains require both tyrosines and strand passage. Our results point towards mechanistic plasticity of gyrase and might pave the way for finding novel and specific mechanism-based gyrase inhibitors." @default.
• W2516230003 created "2016-09-16" @default.
• W2516230003 creator A5010703450 @default.
• W2516230003 creator A5022153527 @default.
• W2516230003 creator A5079760485 @default.
• W2516230003 date "2016-08-23" @default.
• W2516230003 modified "2023-09-25" @default.
• W2516230003 title "DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism" @default.
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• W2516230003 doi "https://doi.org/10.1093/nar/gkw740" @default.
• W2516230003 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5137430" @default.
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• W2516230003 hasPublicationYear "2016" @default.
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