1 research outputs found
Response of the Sensory Animal-like Cryptochrome aCRY to Blue and Red Light As Revealed by Infrared Difference Spectroscopy
Cryptochromes act as blue light sensors
in plants, insects, fungi,
and bacteria. Recently, an animal-like cryptochrome (aCRY) was identified
in the green alga <i>Chlamydomonas reinhardtii</i> by which
gene expression is altered in response to not only blue light but
also yellow and red light. This unique response of a flavoprotein <i>in vivo</i> has been attributed to the fact that the neutral
radical of the flavin chromophore acts as dark form of the sensor,
which absorbs in almost the entire visible spectral range (<680
nm). Here, we investigated light-induced processes in the protein
moiety of full-length aCRY by UV–vis and Fourier transform
infrared spectroscopy. Findings are compared to published results
on the homologous (6-4) photolyases, DNA repair enzymes. The oxidized
state of aCRY is converted to the neutral radical by blue light. The
recovery is strongly dependent on pH and might be catalyzed by a conserved
histidine of the (6-4)/clock cluster. The decay is independent of
oxygen concentration in contrast to that of other cryptochromes and
(6-4) photolyases. This blue light reaction of the oxidized flavin
is not accompanied by any detectable changes in secondary structure,
in agreement with a role <i>in vivo</i> of an unphysiological
preactivation. In contrast, the conversion by red light of the neutral
radical to the anionic fully reduced state proceeds with conformational
changes in turn elements, which most probably constitute a part of
the signaling process. These changes have not been detected in the
corresponding transition of (6-4) photolyase, which points to a decisive
difference between the sensor and the enzyme