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Engineering a Yellow Thermostable Fluorescent Protein by Rational Design
[Image: see text] Thermal green protein (TGP) is an extremely stable, highly soluble synthetic green fluorescent protein. The quantum yield of TGP is lower than the closest related natural fluorescent protein, monomeric Azami-Green. We improved the thermal recovery of TGP through the introduction of...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9835079/ https://www.ncbi.nlm.nih.gov/pubmed/36643458 http://dx.doi.org/10.1021/acsomega.2c05005 |
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author | Anderson, Matthew R. Padgett, Caitlin M. Dargatz, Cammi J. Nichols, Calysta R. Vittalam, Keerti R. DeVore, Natasha M. |
author_facet | Anderson, Matthew R. Padgett, Caitlin M. Dargatz, Cammi J. Nichols, Calysta R. Vittalam, Keerti R. DeVore, Natasha M. |
author_sort | Anderson, Matthew R. |
collection | PubMed |
description | [Image: see text] Thermal green protein (TGP) is an extremely stable, highly soluble synthetic green fluorescent protein. The quantum yield of TGP is lower than the closest related natural fluorescent protein, monomeric Azami-Green. We improved the thermal recovery of TGP through the introduction of a chromophore mutation, Q66E. Furthermore, we developed a yellow thermal protein (YTP) via mutation of histidine 193 to tyrosine. Incorporation of Q66E into YTP (YTP-E) improved chemostability and pH stability. Both YTP and YTP-E have superior thermostability compared to TGP or TGP-E. These proteins offer a new option for green or yellow fluorescence under harsh chemical or thermal conditions. |
format | Online Article Text |
id | pubmed-9835079 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-98350792023-01-13 Engineering a Yellow Thermostable Fluorescent Protein by Rational Design Anderson, Matthew R. Padgett, Caitlin M. Dargatz, Cammi J. Nichols, Calysta R. Vittalam, Keerti R. DeVore, Natasha M. ACS Omega [Image: see text] Thermal green protein (TGP) is an extremely stable, highly soluble synthetic green fluorescent protein. The quantum yield of TGP is lower than the closest related natural fluorescent protein, monomeric Azami-Green. We improved the thermal recovery of TGP through the introduction of a chromophore mutation, Q66E. Furthermore, we developed a yellow thermal protein (YTP) via mutation of histidine 193 to tyrosine. Incorporation of Q66E into YTP (YTP-E) improved chemostability and pH stability. Both YTP and YTP-E have superior thermostability compared to TGP or TGP-E. These proteins offer a new option for green or yellow fluorescence under harsh chemical or thermal conditions. American Chemical Society 2022-12-28 /pmc/articles/PMC9835079/ /pubmed/36643458 http://dx.doi.org/10.1021/acsomega.2c05005 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Anderson, Matthew R. Padgett, Caitlin M. Dargatz, Cammi J. Nichols, Calysta R. Vittalam, Keerti R. DeVore, Natasha M. Engineering a Yellow Thermostable Fluorescent Protein by Rational Design |
title | Engineering a Yellow Thermostable Fluorescent Protein
by Rational Design |
title_full | Engineering a Yellow Thermostable Fluorescent Protein
by Rational Design |
title_fullStr | Engineering a Yellow Thermostable Fluorescent Protein
by Rational Design |
title_full_unstemmed | Engineering a Yellow Thermostable Fluorescent Protein
by Rational Design |
title_short | Engineering a Yellow Thermostable Fluorescent Protein
by Rational Design |
title_sort | engineering a yellow thermostable fluorescent protein
by rational design |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9835079/ https://www.ncbi.nlm.nih.gov/pubmed/36643458 http://dx.doi.org/10.1021/acsomega.2c05005 |
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