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J Plant Physiol. 2015 Jan 1;172:42-54. doi: 10.1016/j.jplph.2014.06.011. Epub 2014 Jul 7.

Dealing with light: the widespread and multitasking cryptochrome/photolyase family in photosynthetic organisms.

Author information

1
Sorbonne Universités, UPMC Univ Paris 06, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France; CNRS, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France.
2
Sorbonne Universités, UPMC Univ Paris 06, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France; CNRS, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France. Electronic address: jean-pierre.bouly@upmc.fr.
3
Sorbonne Universités, UPMC Univ Paris 06, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France; CNRS, UMR 7238, Computational and Quantitative Biology, F-75006 Paris, France. Electronic address: angela.falciatore@upmc.fr.

Abstract

Light is essential for the life of photosynthetic organisms as it is a source of energy and information from the environment. Light excess or limitation can be a cause of stress however. Photosynthetic organisms exhibit sophisticated mechanisms to adjust their physiology and growth to the local environmental light conditions. The cryptochrome/photolyase family (CPF) is composed of flavoproteins with similar structures that display a variety of light-dependent functions. This family encompasses photolyases, blue-light activated enzymes that repair ultraviolet-light induced DNA damage, and cryptochromes, known for their photoreceptor functions in terrestrial plants. For this review, we searched extensively for CPFs in the available genome databases to trace the distribution and evolution of this protein family in photosynthetic organisms. By merging molecular data with current knowledge from the functional characterization of CPFs from terrestrial and aquatic organisms, we discuss their roles in (i) photoperception, (ii) biological rhythm regulation and (iii) light-induced stress responses. We also explore their possible implication in light-related physiological acclimation and their distribution in phototrophs living in different environments. The outcome of this structure-function analysis reconstructs the complex scenarios in which CPFs have evolved, as highlighted by the novel functions and biochemical properties of the most recently described family members in algae.

KEYWORDS:

Cryptochromes; Photolyases; Photoreceptors; UVA/blue light phototrophs

PMID:
25087009
DOI:
10.1016/j.jplph.2014.06.011
[Indexed for MEDLINE]

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