Light-Induced Conformational Changes in the Plant Cryptochrome Photolyase Homology Region Resolved by Selective Isotope Labeling and Infrared Spectroscopy

Photochemistry and Photobiology
Constanze SommerTilman Kottke

Abstract

Plant cryptochromes are photoreceptors that regulate flowering, circadian rhythm and photomorphogenesis in response to blue and UV-A light. It has been demonstrated that the oxidized flavin cofactor is photoreduced to the neutral radical state via separate electron and proton transfer. Conformational changes have been found in the C-terminal extension, but few studies have addressed the changes in secondary structure in the sensory photolyase homology region (PHR). Here, we investigated the PHR of the plant cryptochrome from the green alga Chlamydomonas reinhardtii by light-induced infrared difference spectroscopy in combination with global 13 C and 15 N isotope labeling. Assignment of the signals is achieved by establishing a labeling strategy for cryptochromes that preserves the flavin at natural abundance. We demonstrate by UV/vis spectroscopy that the integrity of the sample is maintained and by mass spectrometry that the global labeling was highly efficient. As a result, difference bands are resolved at full intensity that at natural abundance are compensated by the overlap of flavin and protein signals. These bands are assigned to prominent conformational changes in the PHR by blue light illumination. We postulate that no...Continue Reading

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Citations

Sep 17, 2020·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Tatsuya IwataHideki Kandori
Mar 24, 2020·Chemical Reviews·Victor A Lorenz-Fonfria
Jun 9, 2021·The Journal of Physical Chemistry Letters·Lukas Goett-ZinkTilman Kottke
May 17, 2021·Protein Science : a Publication of the Protein Society·Nischal KarkiBrian D Zoltowski
Jun 20, 2021·Science Advances·Yingjie WangJiali Gao
Jul 10, 2018·Chemical Reviews·Aba LosiAndreas Möglich

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