ArticleOrganic & biomolecular chemistry2019
Efficiency and fidelity of T3 DNA ligase in ligase-catalysed oligonucleotide polymerisations.
Article in Organic & biomolecular chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Template-dependent DNA ligation for the synthesis of modified oligonucleotides.Nature communications · 2024Article
- Ligase-mediated synthesis of CuChemical science · 2024Article
- Advances in ligase-based nucleic acid amplification technology for detecting gene mutations: a review.Molecular and cellular biochemistry · 2023Review
- Generating experimentally unrelated target molecule-binding highly functionalized nucleic-acid polymers using machine learning.Nature communications · 2022Article
- Cognate base-pair selectivity of hydrophobic unnatural bases in DNA ligation by T4 DNA ligase.Biopolymers · 2021Article
- Side chain determinants of biopolymer function during selection and replication.Nature chemical biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Ligase-catalyzed oligonucleotide polymerisations (LOOPER) can readily generate libraries of diversely-modified nucleic acid polymers, which can be subjected to iterative rounds of in vitro selection to evolve functional activity. While there exist several different DNA ligases, T4 DNA ligase has most often been used for the process. Recently, T3 DNA ligase was shown to be effective in LOOPER; however, little is known about the fidelity and efficiency of this enzyme in LOOPER. In this paper we evaluate the efficiency of T3 DNA ligase and T4 DNA ligase for various codon lengths and compositions within the context of polymerisation fidelity and yield. We find that T3 DNA ligase exhibits high efficiency and fidelity with short codon lengths, but struggles with longer and more complex codon libraries, while T4 DNA ligase exhibits the opposite trend. Interestingly, T3 DNA ligase is unable to accommodate modifications at the 8-position of adenosine when integrated into short codons, which will create challenges in expanding the available codon set for the process. The limitations and strengths of the two ligases are further discussed within the context of LOOPER.
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Registered trials
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