Issue 11, 2017

Structure–activity relationships of the ATP cofactor in ligase-catalysed oligonucleotide polymerisations

Abstract

A T4 DNA ligase-catalysed oligonucleotide polymerisation process has been recently developed to enable the incorporation of multiple functional groups throughout a nucleic acid polymer. T4 DNA ligase requires ATP as a cofactor to catalyse phosphodiester bond formation during the polymerisation process. Herein, we describe the structure–activity relationship of ATP within the context of T4 DNA ligase-catalyzed oligonucleotide polymerisation. Using high-throughput sequencing, we study not only the influence of ATP modification on polymerisation efficiency, but also on the fidelity and sequence bias of the polymerisation process.

Graphical abstract: Structure–activity relationships of the ATP cofactor in ligase-catalysed oligonucleotide polymerisations

Supplementary files

Article information

Article type
Communication
Submitted
22 Dec 2016
Accepted
17 Feb 2017
First published
17 Feb 2017

Org. Biomol. Chem., 2017,15, 2349-2352

Structure–activity relationships of the ATP cofactor in ligase-catalysed oligonucleotide polymerisations

Y. Lei and R. Hili, Org. Biomol. Chem., 2017, 15, 2349 DOI: 10.1039/C6OB02792J

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