Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution
Photoconvertible fluorescent proteins (pcFPs) constitute a large group of fluorescent proteins related to green fluorescent protein (GFP) that, when exposed to blue light, bear the capability of irreversibly switching their emission color from green to red. Not surprisingly, this fascinating class o...
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| Format: | Article |
| Language: | English |
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MDPI AG
2017-08-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/18/8/1792 |
| _version_ | 1811231907901341696 |
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| author | Rebekka M. Wachter |
| author_facet | Rebekka M. Wachter |
| author_sort | Rebekka M. Wachter |
| collection | DOAJ |
| description | Photoconvertible fluorescent proteins (pcFPs) constitute a large group of fluorescent proteins related to green fluorescent protein (GFP) that, when exposed to blue light, bear the capability of irreversibly switching their emission color from green to red. Not surprisingly, this fascinating class of FPs has found numerous applications, in particular for the visualization of biological processes. A detailed understanding of the photoconversion mechanism appears indispensable in the design of improved variants for applications such as super-resolution imaging. In this article, recent work is reviewed that involves using pcFPs as a model system for studying protein dynamics. Evidence has been provided that the evolution of pcFPs from a green ancestor involved the natural selection for altered dynamical features of the beta-barrel fold. It appears that photoconversion may be the outcome of a long-range positional shift of a fold-anchoring region. A relatively stiff, rigid element appears to have migrated away from the chromophore-bearing section to the opposite edge of the barrel, thereby endowing pcFPs with increased active site flexibility while keeping the fold intact. In this way, the stage was set for the coupling of light absorption with subsequent chemical transformations. The emerging mechanistic model suggests that highly specific dynamic motions are linked to key chemical steps, preparing the system for a concerted deprotonation and β-elimination reaction that enlarges the chromophore’s π-conjugation to generate red color. |
| first_indexed | 2024-04-12T10:53:57Z |
| format | Article |
| id | doaj.art-1546e8d75e9c4b858737c6b634df08dc |
| institution | Directory Open Access Journal |
| issn | 1422-0067 |
| language | English |
| last_indexed | 2024-04-12T10:53:57Z |
| publishDate | 2017-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-1546e8d75e9c4b858737c6b634df08dc2022-12-22T03:36:08ZengMDPI AGInternational Journal of Molecular Sciences1422-00672017-08-01188179210.3390/ijms18081792ijms18081792Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein EvolutionRebekka M. Wachter0School of Molecular Sciences and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, AZ 85287, USAPhotoconvertible fluorescent proteins (pcFPs) constitute a large group of fluorescent proteins related to green fluorescent protein (GFP) that, when exposed to blue light, bear the capability of irreversibly switching their emission color from green to red. Not surprisingly, this fascinating class of FPs has found numerous applications, in particular for the visualization of biological processes. A detailed understanding of the photoconversion mechanism appears indispensable in the design of improved variants for applications such as super-resolution imaging. In this article, recent work is reviewed that involves using pcFPs as a model system for studying protein dynamics. Evidence has been provided that the evolution of pcFPs from a green ancestor involved the natural selection for altered dynamical features of the beta-barrel fold. It appears that photoconversion may be the outcome of a long-range positional shift of a fold-anchoring region. A relatively stiff, rigid element appears to have migrated away from the chromophore-bearing section to the opposite edge of the barrel, thereby endowing pcFPs with increased active site flexibility while keeping the fold intact. In this way, the stage was set for the coupling of light absorption with subsequent chemical transformations. The emerging mechanistic model suggests that highly specific dynamic motions are linked to key chemical steps, preparing the system for a concerted deprotonation and β-elimination reaction that enlarges the chromophore’s π-conjugation to generate red color.https://www.mdpi.com/1422-0067/18/8/1792green fluorescent proteinproton transferreverse protonation |
| spellingShingle | Rebekka M. Wachter Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution International Journal of Molecular Sciences green fluorescent protein proton transfer reverse protonation |
| title | Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution |
| title_full | Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution |
| title_fullStr | Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution |
| title_full_unstemmed | Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution |
| title_short | Photoconvertible Fluorescent Proteins and the Role of Dynamics in Protein Evolution |
| title_sort | photoconvertible fluorescent proteins and the role of dynamics in protein evolution |
| topic | green fluorescent protein proton transfer reverse protonation |
| url | https://www.mdpi.com/1422-0067/18/8/1792 |
| work_keys_str_mv | AT rebekkamwachter photoconvertiblefluorescentproteinsandtheroleofdynamicsinproteinevolution |