ReviewBiochemical Society transactions2013
Studies of bacterial topoisomerases I and III at the single-molecule level.
Review in Biochemical Society transactions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Molecular dynamics simulations reveal DNA gate opening mechanisms for M. smegmatis topoisomerase 1A.Biophysical journal · 2026Article
- Mechanism of Type IA Topoisomerases.Molecules (Basel, Switzerland) · 2020Review
- A highly processive actinobacterial topoisomerase I - thoughts onMicrobiology (Reading, England) · 2020Review
- Kinetic Study of DNA Topoisomerases by Supercoiling-Dependent Fluorescence Quenching.ACS omega · 2019Article
- Supercoiling of an excised genomic island represses effector gene expression to prevent activation of host resistance.Molecular microbiology · 2018Article
- Investigating mycobacterial topoisomerase I mechanism from the analysis of metal and DNA substrate interactions at the active site.Nucleic acids research · 2018Article
- C-terminal lysine repeats in Streptomyces topoisomerase I stabilize the enzyme-DNA complex and confer high enzyme processivity.Nucleic acids research · 2017Article
- Identification of proximal sites for unwound DNA substrate in Escherichia coli topoisomerase I with oxidative crosslinking.FEBS letters · 2017Article
- The interplay between DNA topology and accessory factors in site-specific recombination in bacteria and their bacteriophages.Science progress · 2016Review
- Insights from the Structure of Mycobacterium tuberculosis Topoisomerase I with a Novel Protein Fold.Journal of molecular biology · 2016Article
- Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I.Nucleic acids research · 2015Article
- Article
- Targeting bacterial topoisomerase I to meet the challenge of finding new antibiotics.Future medicinal chemistry · 2015Review
- DNA Mechanics and Topology.Advances in experimental medicine and biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Topoisomerases are the enzymes responsible for maintaining the supercoiled state of DNA in the cell and also for many other DNA-topology-associated reactions. Type IA enzymes alter DNA topology by breaking one DNA strand and passing another strand or strands through the break. Although all type IA topoisomerases are related at the sequence, structure and mechanism levels, different type IA enzymes do not participate in the same cellular processes. We have studied the mechanism of DNA relaxation by Escherichia coli topoisomerases I and III using single-molecule techniques to understand their dissimilarities. Our experiments show important differences at the single-molecule level, while also recovering the results from bulk experiments. Overall, topoisomerase III relaxes DNA using fast processive runs followed by long pauses, whereas topoisomerase I relaxes DNA through slow processive runs followed by short pauses. These two properties combined give rise to the overall relaxation rate, which is higher for topoisomerase I than for topoisomerase III, as expected from many biochemical observations. The results help us to understand better the role of these two topoisomerases in the cell and also serve to illustrate the power of single-molecule experiments to uncover new functional characteristics of biological molecules.
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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.