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The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser.
Claesson, Elin; Wahlgren, Weixiao Yuan; Takala, Heikki; Pandey, Suraj; Castillon, Leticia; Kuznetsova, Valentyna; Henry, Léocadie; Panman, Matthijs; Carrillo, Melissa; Kübel, Joachim; Nanekar, Rahul; Isaksson, Linnéa; Nimmrich, Amke; Cellini, Andrea; Morozov, Dmitry; Maj, Michal; Kurttila, Moona; Bosman, Robert; Nango, Eriko; Tanaka, Rie; Tanaka, Tomoyuki; Fangjia, Luo; Iwata, So; Owada, Shigeki; Moffat, Keith; Groenhof, Gerrit; Stojkovic, Emina A; Ihalainen, Janne A; Schmidt, Marius; Westenhoff, Sebastian.
Afiliação
  • Claesson E; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Wahlgren WY; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Takala H; Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.
  • Pandey S; Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
  • Castillon L; Physics Department, University of Wisconsin-Milwaukee, Milwaukee, United States.
  • Kuznetsova V; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Henry L; Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.
  • Panman M; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Carrillo M; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Kübel J; Department of Biology, Northeastern Illinois University, Chicago, United States.
  • Nanekar R; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Isaksson L; Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.
  • Nimmrich A; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Cellini A; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Morozov D; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Maj M; Department of Chemistry, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.
  • Kurttila M; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Bosman R; Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland.
  • Nango E; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Tanaka R; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  • Tanaka T; RIKEN SPring-8 Center, Hyogo, Japan.
  • Fangjia L; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  • Iwata S; RIKEN SPring-8 Center, Hyogo, Japan.
  • Owada S; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  • Moffat K; RIKEN SPring-8 Center, Hyogo, Japan.
  • Groenhof G; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  • Stojkovic EA; RIKEN SPring-8 Center, Hyogo, Japan.
  • Ihalainen JA; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  • Schmidt M; RIKEN SPring-8 Center, Hyogo, Japan.
  • Westenhoff S; RIKEN SPring-8 Center, Hyogo, Japan.
Elife ; 92020 03 31.
Article em En | MEDLINE | ID: mdl-32228856
Plants adapt to the availability of light throughout their lives because it regulates so many aspects of their growth and reproduction. To detect the level of light, plant cells use proteins called phytochromes, which are also found in some bacteria and fungi. Phytochrome proteins change shape when they are exposed to red light, and this change alters the behaviour of the cell. The red light is absorbed by a molecule known as chromophore, which is connected to a region of the phytochrome called the PHY-tongue. This region undergoes one of the key structural changes that occur when the phytochrome protein absorbs light, turning from a flat sheet into a helix. Claesson, Wahlgren, Takala et al. studied the structure of a bacterial phytochrome protein almost immediately after shining a very brief flash of red light using a laser. The experiments revealed that the structure of the protein begins to change within a trillionth of a second: specifically, the chromophore twists, which disrupts its attachment to the protein, freeing the protein to change shape. Claesson, Wahlgren, Takala et al. note that this structure is likely a very short-lived intermediate state, which however triggers more changes in the overall shape change of the protein. One feature of the rearrangement is the disappearance of a particular water molecule. This molecule can be found at the core of many different phytochrome structures and interacts with several parts of the chromophore and the phytochrome protein. It is unclear why the water molecule is lost, but given how quickly this happens after the red light is applied it is likely that this disappearance is an integral part of the reshaping process. Together these events disrupt the interactions between the chromophore and the PHY-tongue, enabling the PHY-tongue to change shape and alter the structure of the phytochrome protein. Understanding and controlling this process could allow scientists to alter growth patterns in plants, such as crops or weeds.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fitocromo / Proteínas de Bactérias / Cristalografia por Raios X / Luz Idioma: En Revista: Elife Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Suécia País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fitocromo / Proteínas de Bactérias / Cristalografia por Raios X / Luz Idioma: En Revista: Elife Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Suécia País de publicação: Reino Unido