title: 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.
authors.affiliation: Department of Chemistry, University of Georgia, Athens, GA 30602, USA. rhili@uga.edu.
authors.forename: Yi
authors.initials: Y
authors.lastname: Lei
authors.forename: Ryan
authors.initials: R
authors.lastname: Hili
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D011088:DNA Ligases / Q000378:metabolism*; D015394:Molecular Structure; D009841:Oligonucleotides / Q000096:biosynthesis* / Q000737:chemistry; D058105:Polymerization; D013329:Structure-Activity Relationship
chemical_list: D009841:Oligonucleotides; D000255:Adenosine Triphosphate; D011088:DNA Ligases