ArticleProceedings of the National Academy of Sciences of the United States of America2018
Bottom-up single-molecule strategy for understanding subunit function of tetrameric β-galactosidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia.Science advances · 2026Article
- Anfinsen Redux: Ribonuclease Folding in the Single-Molecule Regime.Journal of the American Chemical Society · 2025Article
- Single-Molecule Enzyme Activity Analysis for Illuminating Pathological Proteoforms.ACS central science · 2025Review
- Single molecule delivery into living cells.Nature communications · 2024Article
- Digital Cascade Assays for ADP- or ATP-Producing Enzymes Using a Femtoliter Reactor Array Device.ACS sensors · 2023Article
- Single-molecule studies reveal method for tuning the heterogeneous activity of alkaline phosphatase.Biophysical journal · 2022Article
- Atlas: automatic modeling of regulation of bacterial gene expression and metabolism using rule-based languages.Bioinformatics (Oxford, England) · 2021Article
- Single-Molecule Mechanistic Study of Enzyme Hysteresis.ACS central science · 2019Article
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
In this paper, we report an example of the engineered expression of tetrameric β-galactosidase (β-gal) containing varying numbers of active monomers. Specifically, by combining wild-type and single-nucleotide polymorphism plasmids at varying ratios, tetrameric β-gal was expressed in vitro with one to four active monomers. The kinetics of individual enzyme molecules revealed four distinct populations, corresponding to the number of active monomers in the enzyme. Using single-molecule-level enzyme kinetics, we were able to measure an accurate in vitro mistranslation frequency (5.8 × 10
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