ArticleBiophysical journal2015
Thermodynamic Protein Destabilization by GFP Tagging: A Case of Interdomain Allostery.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- SDS-22 stabilizes GSP-1/-2 PP1 subunits contributing to polarity establishment in C. elegans embryos.EMBO reports · 2025Article
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Article
- A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Nucleosome proteostasis and histone turnover.Frontiers in molecular biosciences · 2022Review
- GFP fluorescence tagging alters dynamin-related protein 1 oligomerization dynamics and creates disassembly-refractory puncta to mediate mitochondrial fission.Scientific reports · 2020Article
- Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.eLife · 2020Article
- Small-scale approach for precrystallization screening in GPCR X-ray crystallography.Nature protocols · 2020Article
- Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL.Biophysical journal · 2019Article
- Personalized disease signatures through information-theoretic compaction of big cancer data.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.The Journal of biological chemistry · 2017Article
- Development of Series of Affinity Tags in Streptomyces.Scientific reports · 2017Article
- Article
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
The Engrailed Homeodomain (EnHD) transcription factor of Drosophila melanogaster was fused to the enhanced green fluorescent protein (eGFP) either at its C- or N-terminus via three- or ten-residue flexible linkers. Here, we show that EnHD undergoes destabilization upon fusing it to eGFP regardless of the linker length used and whether the tethering is to its N- or C-terminus. The destabilization is reflected in melting points that are lower by up to 9°C. Thermodynamic analysis and coarse-grained molecular dynamic simulations indicate that this destabilization is due to eGFP-promoted entropic stabilization of the denatured state ensemble of EnHD. Our results provide, therefore, an example for destabilizing interdomain allostery. They are also important given the widespread use of eGFP tagging in cell biology, as they indicate that such tagging can cause unintended protein destabilization and concomitant effects.
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