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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.

SUBMITTER: Lei Y

PROVIDER: S-EPMC5419680 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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

Lei Yi Y Hili Ryan R

Organic & biomolecular chemistry 20170228 11

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 ...[more]

PMID: 28244520

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