ArticleACS chemical biology2016
Cysteine Sulfoxidation Increases the Photostability of Red Fluorescent Proteins.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Biospecific Chemistry for Covalent Linking of Biomacromolecules.Chemical reviews · 2024Review
- The role of cysteine residues in the allosteric modulation of the chromophore phototransformations of biphotochromic fluorescent protein SAASoti.Scientific reports · 2021Article
- Visualization of cytoplasmic organelles via in-resin CLEM using an osmium-resistant far-red protein.Scientific reports · 2020Article
- Expression and Characterization of a Bright Far-red Fluorescent Protein from the Pink-Pigmented Tissues of Porites lobata.Marine biotechnology (New York, N.Y.) · 2020Article
- Monomerization of far-red fluorescent proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Light-induced oxidant production by fluorescent proteins.Free radical biology & medicine · 2018Review
- Enhancing fluorescent protein photostability through robot-assisted photobleaching.Integrative biology : quantitative biosciences from nano to macro · 2018Article
- A guide to choosing fluorescent protein combinations for flow cytometric analysis based on spectral overlap.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2018Article
- Genetically encoded fluorescent tags.Molecular biology of the cell · 2017Article
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Authors and funding
6 authors.
Funding
Abstract
Photobleaching of fluorescent proteins (FPs) is a major limitation to their use in advanced microscopy, and improving photostability remains highly challenging due to limited understanding of its molecular mechanism. Here we discovered a new mechanism to increase FP photostability. Cysteine oxidation, implicated in only photobleaching before, was found to drastically enhance FP photostability to the contrary. We generated a far-red FP mStable by introducing a cysteine proximal to the chromophore. Upon illumination, this cysteine was oxidized to sulfinic and sulfonic acids, enabling mStable more photostable than its ancestor mKate2 by 12-fold and surpassing other far-red FPs. mStable outperformed in laser scanning confocal imaging and super-resolution structured illumination microscopy. Moreover, photosensitization to oxidize a cysteine similarly introduced in another FP mPlum also increased its photostability by 23-fold. This postfolding cysteine sulfoxidation cannot be simply substituted by the isosteric aspartic acid, representing a unique mechanism valuable for engineering better photostability into FPs.
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