ArticleBiochemistry2013
A circularly permuted photoactive yellow protein as a scaffold for photoswitch design.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021Article
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- A Yeast System for Discovering Optogenetic Inhibitors of Eukaryotic Translation Initiation.ACS synthetic biology · 2019Article
- Regulation of Protein Structural Changes by Incorporation of a Small-Molecule Linker.International journal of molecular sciences · 2018Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Optogenetic Inhibitor of the Transcription Factor CREB.Chemistry & biology · 2015Article
- Optimizing optogenetic constructs for control over signaling and cell behaviours.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2015Review
- Multiscale approach to the determination of the photoactive yellow protein signaling state ensemble.PLoS computational biology · 2014Article
- Optical control of protein-protein interactions via blue light-induced domain swapping.Biochemistry · 2014Article
- Origins of the Intermediate Spectral Form in M100 Mutants of Photoactive Yellow Protein.Photochemistry and photobiologyArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Upon blue light irradiation, photoactive yellow protein (PYP) undergoes a conformational change that involves large movements at the N-terminus of the protein. We reasoned that this conformational change might be used to control other protein or peptide sequences if these were introduced as linkers connecting the N- and C-termini of PYP in a circular permutant. For such a design strategy to succeed, the circularly permuted PYP (cPYP) would have to fold normally and undergo a photocycle similar to that of the wild-type protein. We created a test cPYP by connecting the N- and C-termini of wild-type PYP (wtPYP) with a GGSGGSGG linker polypeptide and introducing new N- and C-termini at G115 and S114, respectively. Biophysical analysis indicated that this cPYP adopts a dark-state conformation much like wtPYP and undergoes wtPYP-like photoisomerization driven by blue light. However, thermal recovery of dark-state cPYP is ∼10-fold faster than that of wtPYP, so that very bright light is required to significantly populate the light state. Targeted mutations at M121E (M100 in wtPYP numbering) were found to enhance the light sensitivity substantially by lengthening the lifetime of the light state to ∼10 min. Nuclear magnetic resonance (NMR), circular dichroism, and UV-vis analysis indicated that the M121E-cPYP mutant also adopts a dark-state structure like that of wtPYP, although protonated and deprotonated forms of the chromophore coexist, giving rise to a shoulder near 380 nm in the UV-vis absorption spectrum. Fluorine NMR studies with fluorotryptophan-labeled M121E-cPYP show that blue light drives large changes in conformational dynamics and leads to solvent exposure of Trp7 (Trp119 in wtPYP numbering), consistent with substantial rearrangement of the N-terminal cap structure. M121E-cPYP thus provides a scaffold that may allow a wider range of photoswitchable protein designs via replacement of the linker polypeptide with a target protein or peptide sequence.
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