ArticleJACS Au2022
Mechanism-Based Strategy for Optimizing HaloTag Protein Labeling.
Article in JACS Au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- HaloTag-Based FACS-Compatible Assay for Intracellular Haloalkane Detection with a Potential Application to Halogenase Screening.Analytical chemistry · 2026Article
- Molecular rotor-based probes for protein monitoring in biomedical research.Nature reviews. Chemistry · 2026Review
- Two-photon characterisation of long-Stokes-shift dye ATTO 490LS for single-laser multicolour imaging.microPublication biology · 2026Article
- Optimizing multifunctional fluorescent ligands for intracellular labeling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fluorescence Lifetime Multiplexing with Environment-Sensitive Chemigenetic Probes.Chembiochem : a European journal of chemical biology · 2025Article
- To activate a G protein-coupled receptor permanently with cell surface photodynamic action in the gastrointestinal tract.World journal of gastroenterology · 2025Review
- Impact of water models on the structure and dynamics of enzyme tunnels.Computational and structural biotechnology journal · 2024Article
- BenzoHTag, a fluorogenic self-labeling protein developed using molecular evolution.bioRxiv : the preprint server for biology · 2024Article
- Opticool: Cutting-edge transgenic optical tools.PLoS genetics · 2024Review
- Harmony of Protein Tags and Chimeric Molecules Empowers Targeted Protein Ubiquitination and Beyond.Cells · 2024Review
- Engineered fluorogenic HaloTag ligands for turn-on labelling in live cells.Chemical communications (Cambridge, England) · 2023Article
- Atypical homodimerization revealed by the structure of the (S)-enantioselective haloalkane dehalogenase DmmarA from Mycobacterium marinum.Acta crystallographica. Section D, Structural biology · 2023Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
HaloTag labeling technology has introduced unrivaled potential in protein chemistry and molecular and cellular biology. A wide variety of ligands have been developed to meet the specific needs of diverse applications, but only a single protein tag, DhaAHT, is routinely used for their incorporation. Following a systematic kinetic and computational analysis of different reporters, a tetramethylrhodamine- and three 4-stilbazolium-based fluorescent ligands, we showed that the mechanism of incorporating different ligands depends both on the binding step and the efficiency of the chemical reaction. By studying the different haloalkane dehalogenases DhaA, LinB, and DmmA, we found that the architecture of the access tunnels is critical for the kinetics of both steps and the ligand specificity. We showed that highly efficient labeling with specific ligands is achievable with natural dehalogenases. We propose a simple protocol for selecting the optimal protein tag for a specific ligand from the wide pool of available enzymes with diverse access tunnel architectures. The application of this protocol eliminates the need for expensive and laborious protein engineering.
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Registered trials
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