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• W2010129266 abstract "Phage T7 DNA ligase seals nicked DNA substrates and is a representative member of the ATP-dependent class of DNA ligases. Although the catalytic mechanism of DNA ligases has been delineated, little is known about the nature of nick recognition by these enzymes. Here, we show that T7 ligase discriminates, at the nick-binding step, between nicks containing either a 5'-phosphate or a 5'-OH. T7 ligase binds preferentially to phosphorylated nicks and catalyses the sealing reaction. We also show using DNA footprinting studies, that T7 ligase binds asymmetrically to nicks as a monomer, with the protein interface covering between 12 and 14 bp of DNA. Based on molecular modelling studies we propose a structural model of the ligase-DNA complex consistent with these and other data. Using photo-crosslinking and site-directed mutagenesis we have identified two residues, K238 and K240, critical for the transadenylation and nick-sealing reactions. Sequence conservation and structural analysis supports the premise that these two lysine residues are critical for both nucleotide binding and DNA nick recognition. The implications of these results on the ligation mechanism are discussed." @default.
• W2010129266 created "2016-06-24" @default.
• W2010129266 creator A5004063906 @default.
• W2010129266 creator A5055888908 @default.
• W2010129266 date "2000-02-01" @default.
• W2010129266 modified "2023-10-13" @default.
• W2010129266 title "Nick recognition by DNA ligases 1 1Edited by K. Nagai" @default.
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• W2010129266 doi "https://doi.org/10.1006/jmbi.1999.3423" @default.
• W2010129266 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10656817" @default.
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