Browsing by Subject "PHOTOACTIVATION"

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  • Donner, Kristian; Zak, Pavel; Viljanen, Martta; Lindström, Magnus; Feldman, Tatiana; Ostrovsky, Mikhail (2016)
    Absorbance spectra of single rhabdoms were studied by microspectrophotometry (MSP) and spectral sensitivities of whole eyes by electroretinography (ERG) in three glacial-relict species of opossum shrimps (Mysis). Among eight populations from Fennoscandian fresh-water lakes (L) and seven populations from the brackish-water Baltic Sea (S), L spectra were systematically red-shifted by 20-30 nm compared with S spectra, save for one L and one S population. The difference holds across species and bears no consistent adaptive relation to the current light environments. In the most extensively studied L-S pair, two populations of M. relicta (L (p) and S (p)) separated for less than 10,000 years, no differences translating into amino acid substitutions have been found in the opsin genes, and the chromophore of the visual pigments as analyzed by HPLC is pure A1. However, MSP experiments with spectrally selective bleaching show the presence of two rhodopsins (lambda (max) a parts per thousand 525-530 nm, MWS, and 565-570 nm, LWS) expressed in different proportions. ERG recordings of responses to "red" and "blue" light linearly polarized at orthogonal angles indicate segregation of the pigments into different cells differing in polarization sensitivity. We propose that the pattern of development of LWS and MWS photoreceptors is governed by an ontogenetic switch responsive to some environmental signal(s) other than light that generally differ(s) between lakes and sea, and that this reaction norm is conserved from a common ancestor of all three species.
  • Cellini, Andrea; Wahlgren, Weixiao Yuan; Henry, Leocadie; Pandey, Suraj; Ghosh, Swagatha; Castillon, Leticia; Claesson, Elin; Takala, Heikki; Kubel, Joachim; Nimmrich, Amke; Kuznetsova, Valentyna; Nango, Eriko; Iwata, So; Owada, Shigeki; Stojkovic, Emina A.; Schmidt, Marius; Ihalainen, Janne A.; Westenhoff, Sebastian (2021)
    (6-4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6-4) photolyase [Dm(6-4)photolyase] at room and cryogenic temperatures are reported. The room-temperature structure was solved to 2.27 angstrom resolution and was obtained by serial femtosecond crystallography (SFX) using an X-ray free-electron laser. The crystallization and preparation conditions are also reported. The cryogenic structure was solved to 1.79 angstrom resolution using conventional X-ray crystallography. The structures agree with each other, indicating that the structural information obtained from crystallography at cryogenic temperature also applies at room temperature. Furthermore, UV-Vis absorption spectroscopy confirms that Dm(6-4)photolyase is photoactive in the crystals, giving a green light to time-resolved SFX studies on the protein, which can reveal the structural mechanism of the photoactivated protein in DNA repair.