Structural and functional relationships of plant cryptochromes

• Antragsteller: Professor Dr. Alfred Batschauer
• Fachliche Zuordnung: Biophysik
• Förderung: Förderung von 2004 bis 2011
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5470629

• Erstellungsjahr: 2012

Zusammenfassung der Projektergebnisse

Cryptochromes together with DNA photolyases constitute a large protein family of flavoproteins that are present in all kingdoms of life. Whereas DNA photolyases repair the major UV-B lesions in DNA, cryptochromes function as UV-A/blue light photoreceptors and have normally no photolyase activity. However, there are some exceptions to this rule with family members having a dual role in repair and signaling. Moreover, there is evidence that cryptochromes could function as magnetoreceptors which depend on photoexcitation. Our focus within this research unit was on a detailed understanding of how such closely related proteins as photolyase and cryptochrome fulfill very different biological functions, namely electron-mediated catalysis using fully reduced and light-excited FADH-* or light signaling from the lid state that contains semireduced FAD. These studies were mostly done in an interdisciplinary approach on members of the cryptochrome/photolyase family from Arabidopsis thaliana and resulted in a multitude of published structural, spectroscopic and functional data.

Projektbezogene Publikationen (Auswahl)

• (2005) Crystallization and preliminary X-ray analysis of cryptochrome 3 from Arabidopsis thaliana. Acta Crys. F61, 935-938
  Pokorny, Richard; Klar, Tobias; Essen, Lars-Oliver & Batschauer, Alfred
  
• (2006) Absorption and fluorescence spectroscopic characterization of cryptochrome 3 from Arabidopsis thaliana. J. Photochem. Photobiol. B: Biol. 85, 1-6
  Song, S.-H.; Dick, B.; Penzkofer, A.; Pokorny, R.; Batschauer, A. & Essen, L.-O.
  
• (2006) Blue-light induced changes in cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry 45, 2472-2479
  Kottke, Tilman; Batschauer, Alfred; Ahmad, Margaret & Heberle, Joachim
  
• (2006) Natural and non-natural chromophores in the DNA photolyase from Thermus thermophilus. ChemBioChem. 7, 1798-1806
  Klar, Tobias; Kaiser, Gebhard; Hennecke, Ulrich; Carell, Thomas; Batschauer, Alfred & Essen, Lars‐Oliver
  
• (2007) Cryptochrome 3 from Arabidopsis thaliana: Structural and functional analysis of its complex with a folate light antenna. J. Mol. Biol. 366, 954-964
  Klar, Tobias; Pokorny, Richard; Moldt, Julia; Batschauer, Alfred & Essen, Lars-Oliver
  
• (2007) Cryptochrome blue-light photoreceptors are activated through interconversion of flavin redox states. J. Biol. Chem. 282, 9383-9391
  Bouly, Jean-Pierre; Schleicher, Erik; Dionisio-Sese, Maribel; Vandenbussche, Filip; Van Der Straeten, Dominique; Bakrim, Nadia; Meier, Stefan; Batschauer, Alfred; Galland, Paul; Bittl, Robert & Ahmad, Margaret
  
• (2007) The signaling state of Arabidopsis cryptochrome 2 contains flavin semiquinone. J. Biol. Chem. 282, 14916-14922
  Banerjee, Roopa; Schleicher, Erik; Meier, Stefan; Viana, Rafael Muñoz; Pokorny, Richard; Ahmad, Margaret; Bittl, Robert & Batschauer, Alfred
  
• (2008) Recognition and repair of UV-lesions in loop structures of duplex DNA by DASH-type cryptochrome. Proc. Natl. Acad. Sci. USA 105, 21023-21027
  Pokorny, Richard; Klar, Tobias; Hennecke, Ulrich; Carell, Thomas; Batschauer, Alfred & Essen, Lars-Oliver
  
• (2009) A cryptochrome-like protein is involved in the regulation of photosynthesis genes in Rhodobacter sphaeroides. Mol. Microbiol. 74, 990-1003
  Hendrischk, Anne‐Kathrin; Frühwirth, Sebastian Walter; Moldt, Julia; Pokorny, Richard; Metz, Sebastian; Kaiser, Gebhard; Jäger, Andreas; Batschauer, Alfred & Klug, Gabriele
  
• (2009) Fluorescence Behaviour of 5,10- Methenyltetrahydrofolate, 10-Formyltetrahydrofolate, 10-Formyldihydrofolate, and 10-Formylfolate in Aqueous Solution at pH 8 Chem. Phys. 361, 75-82
  Tyagi, A.; Penzkofer, A.; Batschauer, A. & Wolf, E.
  
• (2009) Photorededuction of the folate cofactor in members of the photolyase family. J. Biol. Chem. 284, 21670-21683
  Moldt, Julia; Pokorny, Richard; Orth, Christian; Linne, Uwe; Geisselbrecht, Yann; Marahiel, Mohamed A.; Essen, Lars-Oliver & Batschauer, Alfred
  
• (2009) Thermal degradation of (6R,S)-5,10- methenyltetrahydrofolate in aequeos solution at pH 8. Chem. Phys. 358, 132-136
  Tyagi, A.; Penzkofer, A.; Batschauer, A. & Wolf, E.
  
• (2009). Photocycle dynamics of the E149A mutant of cryptochrome 3 from Arabidopsis thaliana. J. Photochem. Photobiol. B: Biol. 97, 94-108
  Zirak, P.; Penzkofer, A.; Moldt, J.; Pokorny, R.; Batschauer, A. & Essen, L.-O.
  
• (2010) The electronic state of flavoproteins: Investigations with proton electronnuclear double resonance. Appl. Magn. Reson. 37, 339-352
  Schleicher, Erik; Wenzel, Ringo; Ahmad, Margret; Batschauer, Alfred; Essen, Lars-Oliver; Hitomi, Kenichi; Getzoff, Elizabeth D.; Bittl, Robert; Weber, Stefan & Okafuji, Asako
  
• (2010) A gain-of-function mutation of Arabidopsis CRYPTOCHROME 1 promotes flowering. Plant Physiol.
  Exner, Vivien; Alexandre, Cristina; Rosenfeldt, Gesa; Alfarano, Pietro; Nater, Mena; Caflisch, Amedeo; Gruissem, Wilhelm; Batschauer, Alfred & Hennig, Lars
  
• (2010) Light-induced activation of class II cyclobutane pyrimidine dimer photolyases. DNA Repair, 9, 495-505
  Okafuji, Asako; Biskup, Till; Hitomi, Kenichi; Getzoff, Elizabeth D.; Kaiser, Gebhard; Batschauer, Alfred; Bacher, Adelbert; Hidema, Jun; Teranishi, Mika; Yamamoto, Kazuo; Schleicher, Erik & Weber, Stefan