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Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome
Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectr...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6126659/ https://www.ncbi.nlm.nih.gov/pubmed/30224965 http://dx.doi.org/10.1107/S2052252518010631 |
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author | Woitowich, Nicole C. Halavaty, Andrei S. Waltz, Patricia Kupitz, Christopher Valera, Joseph Tracy, Gregory Gallagher, Kevin D. Claesson, Elin Nakane, Takanori Pandey, Suraj Nelson, Garrett Tanaka, Rie Nango, Eriko Mizohata, Eiichi Owada, Shigeki Tono, Kensure Joti, Yasumasa Nugent, Angela C. Patel, Hardik Mapara, Ayesha Hopkins, James Duong, Phu Bizhga, Dorina Kovaleva, Svetlana E. St. Peter, Rachael Hernandez, Cynthia N. Ozarowski, Wesley B. Roy-Chowdhuri, Shatabdi Yang, Jay-How Edlund, Petra Takala, Heikki Ihalainen, Janne Brayshaw, Jennifer Norwood, Tyler Poudyal, Ishwor Fromme, Petra Spence, John C. H. Moffat, Keith Westenhoff, Sebastian Schmidt, Marius Stojković, Emina A. |
author_facet | Woitowich, Nicole C. Halavaty, Andrei S. Waltz, Patricia Kupitz, Christopher Valera, Joseph Tracy, Gregory Gallagher, Kevin D. Claesson, Elin Nakane, Takanori Pandey, Suraj Nelson, Garrett Tanaka, Rie Nango, Eriko Mizohata, Eiichi Owada, Shigeki Tono, Kensure Joti, Yasumasa Nugent, Angela C. Patel, Hardik Mapara, Ayesha Hopkins, James Duong, Phu Bizhga, Dorina Kovaleva, Svetlana E. St. Peter, Rachael Hernandez, Cynthia N. Ozarowski, Wesley B. Roy-Chowdhuri, Shatabdi Yang, Jay-How Edlund, Petra Takala, Heikki Ihalainen, Janne Brayshaw, Jennifer Norwood, Tyler Poudyal, Ishwor Fromme, Petra Spence, John C. H. Moffat, Keith Westenhoff, Sebastian Schmidt, Marius Stojković, Emina A. |
author_sort | Woitowich, Nicole C. |
collection | PubMed |
description | Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium. |
format | Online Article Text |
id | pubmed-6126659 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-61266592018-09-17 Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome Woitowich, Nicole C. Halavaty, Andrei S. Waltz, Patricia Kupitz, Christopher Valera, Joseph Tracy, Gregory Gallagher, Kevin D. Claesson, Elin Nakane, Takanori Pandey, Suraj Nelson, Garrett Tanaka, Rie Nango, Eriko Mizohata, Eiichi Owada, Shigeki Tono, Kensure Joti, Yasumasa Nugent, Angela C. Patel, Hardik Mapara, Ayesha Hopkins, James Duong, Phu Bizhga, Dorina Kovaleva, Svetlana E. St. Peter, Rachael Hernandez, Cynthia N. Ozarowski, Wesley B. Roy-Chowdhuri, Shatabdi Yang, Jay-How Edlund, Petra Takala, Heikki Ihalainen, Janne Brayshaw, Jennifer Norwood, Tyler Poudyal, Ishwor Fromme, Petra Spence, John C. H. Moffat, Keith Westenhoff, Sebastian Schmidt, Marius Stojković, Emina A. IUCrJ Research Papers Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium. International Union of Crystallography 2018-08-29 /pmc/articles/PMC6126659/ /pubmed/30224965 http://dx.doi.org/10.1107/S2052252518010631 Text en © Nicole C. Woitowich et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Papers Woitowich, Nicole C. Halavaty, Andrei S. Waltz, Patricia Kupitz, Christopher Valera, Joseph Tracy, Gregory Gallagher, Kevin D. Claesson, Elin Nakane, Takanori Pandey, Suraj Nelson, Garrett Tanaka, Rie Nango, Eriko Mizohata, Eiichi Owada, Shigeki Tono, Kensure Joti, Yasumasa Nugent, Angela C. Patel, Hardik Mapara, Ayesha Hopkins, James Duong, Phu Bizhga, Dorina Kovaleva, Svetlana E. St. Peter, Rachael Hernandez, Cynthia N. Ozarowski, Wesley B. Roy-Chowdhuri, Shatabdi Yang, Jay-How Edlund, Petra Takala, Heikki Ihalainen, Janne Brayshaw, Jennifer Norwood, Tyler Poudyal, Ishwor Fromme, Petra Spence, John C. H. Moffat, Keith Westenhoff, Sebastian Schmidt, Marius Stojković, Emina A. Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title | Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title_full | Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title_fullStr | Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title_full_unstemmed | Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title_short | Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
title_sort | structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6126659/ https://www.ncbi.nlm.nih.gov/pubmed/30224965 http://dx.doi.org/10.1107/S2052252518010631 |
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