Phytochrome-Interacting Proteins
Phytochromes are photoreceptors of plants, fungi, slime molds bacteria and heterokonts. These biliproteins sense red and far-red light and undergo light-induced changes between the two spectral forms, Pr and Pfr. Photoconversion triggered by light induces conformational changes in the bilin chromoph...
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MDPI AG
2023-12-01
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Series: | Biomolecules |
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Online Access: | https://www.mdpi.com/2218-273X/14/1/9 |
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author | Gero Kaeser Norbert Krauß Clare Roughan Luisa Sauthof Patrick Scheerer Tilman Lamparter |
author_facet | Gero Kaeser Norbert Krauß Clare Roughan Luisa Sauthof Patrick Scheerer Tilman Lamparter |
author_sort | Gero Kaeser |
collection | DOAJ |
description | Phytochromes are photoreceptors of plants, fungi, slime molds bacteria and heterokonts. These biliproteins sense red and far-red light and undergo light-induced changes between the two spectral forms, Pr and Pfr. Photoconversion triggered by light induces conformational changes in the bilin chromophore around the ring C-D-connecting methine bridge and is followed by conformational changes in the protein. For plant phytochromes, multiple phytochrome interacting proteins that mediate signal transduction, nuclear translocation or protein degradation have been identified. Few interacting proteins are known as bacterial or fungal phytochromes. Here, we describe how the interacting partners were identified, what is known about the different interactions and in which context of signal transduction these interactions are to be seen. The three-dimensional arrangement of these interacting partners is not known. Using an artificial intelligence system-based modeling software, a few predicted and modulated examples of interactions of bacterial phytochromes with their interaction partners are interpreted. |
first_indexed | 2024-03-08T11:04:53Z |
format | Article |
id | doaj.art-ee53b42fdf2445ff9091a139114ca653 |
institution | Directory Open Access Journal |
issn | 2218-273X |
language | English |
last_indexed | 2024-03-08T11:04:53Z |
publishDate | 2023-12-01 |
publisher | MDPI AG |
record_format | Article |
series | Biomolecules |
spelling | doaj.art-ee53b42fdf2445ff9091a139114ca6532024-01-26T15:17:30ZengMDPI AGBiomolecules2218-273X2023-12-01141910.3390/biom14010009Phytochrome-Interacting ProteinsGero Kaeser0Norbert Krauß1Clare Roughan2Luisa Sauthof3Patrick Scheerer4Tilman Lamparter5Karlsruhe Institute of Technology (KIT), Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Fritz-Haber-Weg 4, D-76131 Karlsruhe, GermanyKarlsruhe Institute of Technology (KIT), Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Fritz-Haber-Weg 4, D-76131 Karlsruhe, GermanyKarlsruhe Institute of Technology (KIT), Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Fritz-Haber-Weg 4, D-76131 Karlsruhe, GermanyCharité—Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Structural Biology of Cellular Signaling, Charitéplatz 1, D-10117 Berlin, GermanyCharité—Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Structural Biology of Cellular Signaling, Charitéplatz 1, D-10117 Berlin, GermanyKarlsruhe Institute of Technology (KIT), Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Fritz-Haber-Weg 4, D-76131 Karlsruhe, GermanyPhytochromes are photoreceptors of plants, fungi, slime molds bacteria and heterokonts. These biliproteins sense red and far-red light and undergo light-induced changes between the two spectral forms, Pr and Pfr. Photoconversion triggered by light induces conformational changes in the bilin chromophore around the ring C-D-connecting methine bridge and is followed by conformational changes in the protein. For plant phytochromes, multiple phytochrome interacting proteins that mediate signal transduction, nuclear translocation or protein degradation have been identified. Few interacting proteins are known as bacterial or fungal phytochromes. Here, we describe how the interacting partners were identified, what is known about the different interactions and in which context of signal transduction these interactions are to be seen. The three-dimensional arrangement of these interacting partners is not known. Using an artificial intelligence system-based modeling software, a few predicted and modulated examples of interactions of bacterial phytochromes with their interaction partners are interpreted.https://www.mdpi.com/2218-273X/14/1/9PIF3PKS2Cryplantbacterialfungal |
spellingShingle | Gero Kaeser Norbert Krauß Clare Roughan Luisa Sauthof Patrick Scheerer Tilman Lamparter Phytochrome-Interacting Proteins Biomolecules PIF3 PKS2 Cry plant bacterial fungal |
title | Phytochrome-Interacting Proteins |
title_full | Phytochrome-Interacting Proteins |
title_fullStr | Phytochrome-Interacting Proteins |
title_full_unstemmed | Phytochrome-Interacting Proteins |
title_short | Phytochrome-Interacting Proteins |
title_sort | phytochrome interacting proteins |
topic | PIF3 PKS2 Cry plant bacterial fungal |
url | https://www.mdpi.com/2218-273X/14/1/9 |
work_keys_str_mv | AT gerokaeser phytochromeinteractingproteins AT norbertkrauß phytochromeinteractingproteins AT clareroughan phytochromeinteractingproteins AT luisasauthof phytochromeinteractingproteins AT patrickscheerer phytochromeinteractingproteins AT tilmanlamparter phytochromeinteractingproteins |