ArticleNucleic acids research2001
Overexpression, purification and characterization of RecJ protein from Thermus thermophilus HB8 and its core domain.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Compartmentalized Suspension Array for the Isothermal, Digital, and Multiplex Detection of microRNAs.Journal of the American Chemical Society · 2025Article
- Functional analysis of single enzymes combining programmable molecular circuits with droplet-based microfluidics.Nature nanotechnology · 2024Article
- Differential requirement for RecFOR pathway components in Thermus thermophilus.Environmental microbiology reports · 2024Article
- Coupling Exponential to Linear Amplification for Endpoint Quantitative Analysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Deletion of the primase-polymerases encoding gene, located in a mobile element inFrontiers in microbiology · 2022Article
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- Isothermal digital detection of microRNAs using background-free molecular circuit.Science advances · 2020Article
- The trimeric Hef-associated nuclease HAN is a 3'→5' exonuclease and is probably involved in DNA repair.Nucleic acids research · 2018Article
- Boosting functionality of synthetic DNA circuits with tailored deactivation.Nature communications · 2016Article
- High-resolution mapping of bifurcations in nonlinear biochemical circuits.Nature chemistry · 2016Article
- Role of RecJ-like protein with 5'-3' exonuclease activity in oligo(deoxy)nucleotide degradation.The Journal of biological chemistry · 2011Article
- Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systems.Journal of nucleic acids · 2010Article
- A novel single-stranded DNA-specific 3'-5' exonuclease, Thermus thermophilus exonuclease I, is involved in several DNA repair pathways.Nucleic acids research · 2010Article
- DNA mismatch repair in eukaryotes and bacteria.Journal of nucleic acids · 2010Article
- Structure of RecJ exonuclease defines its specificity for single-stranded DNA.The Journal of biological chemistry · 2010Article
- YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity.The Journal of biological chemistry · 2010Article
- RecJ exonuclease: substrates, products and interaction with SSB.Nucleic acids research · 2006Article
- Engineering and functional evaluation of a single-chain antibody against HIV-1 external glycoprotein gp120.Clinical and experimental immunology · 2005Article
- The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A recJ homolog was cloned from the extremely thermophilic bacterium Thermus themophilus HB8. It encodes a 527 amino acid protein that has 33% identity to Escherichia coli RecJ protein and includes the characteristic motifs conserved among RecJ homologs. Although T.thermophilus RecJ protein (ttRecJ) was expressed as an inclusion body, it was purified in soluble form through denaturation with urea and subsequent refolding steps. Limited proteolysis showed that ttRecJ has a protease-resistant core domain, which includes all the conserved motifs. We constructed a truncated ttRecJ gene that corresponds to the core domain (cd-ttRecJ). cd-ttRecJ was overexpressed in soluble form and purified. ttRecJ and cd-ttRecJ were stable up to 60 degrees C. Size exclusion chromatography indicated that ttRecJ exists in several oligomeric states, whereas cd-ttRecJ is monomeric in solution. Both proteins have 5'-->3' exonuclease activity, which was enhanced by increasing the temperature to 50 degrees C. Mg(2+), Mn(2+) or Co(2+) ions were required to activate both proteins, whereas Ca(2+) and Zn(2+) had no effects.
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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.