ArticleMolecular biotechnology1998
High-level expression of murine terminal deoxynucleotidyl transferase in Escherichia coli grown at low temperature and overexpressing argU tRNA.
Article in Molecular biotechnology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Optimization of Expression and Thermostability of Terminal Deoxynucleotidyl Transferase Through Iterative Mutagenesis and Computational Design.Applied biochemistry and biotechnology · 2026Article
- Terminal deoxynucleotidyl transferase: Properties and applications.Engineering microbiology · 2025Review
- Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.Nature communications · 2024Article
- Recording Temporal Signals with Minutes Resolution Using Enzymatic DNA Synthesis.Journal of the American Chemical Society · 2021Article
- Enzymatic synthesis and modification of high molecular weight DNA using terminal deoxynucleotidyl transferase.Methods in enzymology · 2019Article
- De novo DNA synthesis using polymerase-nucleotide conjugates.Nature biotechnology · 2018Article
- Terminal deoxynucleotidyl transferase requires KU80 and XRCC4 to promote N-addition at non-V(D)J chromosomal breaks in non-lymphoid cells.Nucleic acids research · 2012Article
- Terminal deoxynucleotidyl transferase: the story of a misguided DNA polymerase.Biochimica et biophysica acta · 2010Review
- Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region.Nucleic acids research · 2009Article
- Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terminal deoxynucleotidyl transferase (TdT) is a highly conserved vertebrate enzyme that possesses the unique ability to catalyze the random addition of deoxynucleoside 5'-triphosphates onto the 3'-hydroxyl group of a single-stranded DNA. It plays an important role in the generation of immunoglobin and T-cell receptor diversity. TdT is usually obtained from animal thymus gland or produced in a baculovirus system, but both procedures are rather tedious, and proteolysis occurs during purification. Attempts to overexpress TdT in bacteria have been unsuccessful or have yielded an enzyme with a lower specific activity. A dearth of TdT has thus hampered detailed structural and functional studies. In the present study, we report that by lowering growth temperature and overexpressing a rare arginyl tRNA, it is possible to boost the production in Escherichia coli of murine TdT with minimal proteolysis and high specific activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.