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2015 ; 10
(9
): e0135940
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Evolutionary History of the Photolyase/Cryptochrome Superfamily in Eukaryotes
#MMPMID26352435
Mei Q
; Dvornyk V
PLoS One
2015[]; 10
(9
): e0135940
PMID26352435
show ga
BACKGROUND: Photolyases and cryptochromes are evolutionarily related
flavoproteins, which however perform distinct physiological functions.
Photolyases (PHR) are evolutionarily ancient enzymes. They are activated by light
and repair DNA damage caused by UV radiation. Although cryptochromes share
structural similarity with DNA photolyases, they lack DNA repair activity.
Cryptochrome (CRY) is one of the key elements of the circadian system in animals.
In plants, CRY acts as a blue light receptor to entrain circadian rhythms, and
mediates a variety of light responses, such as the regulation of flowering and
seedling growth. RESULTS: We performed a comprehensive evolutionary analysis of
the CRY/PHR superfamily. The superfamily consists of 7 major subfamilies: CPD
class I and CPD class II photolyases, (6-4) photolyases, CRY-DASH, plant PHR2,
plant CRY and animal CRY. Although the whole superfamily evolved primarily under
strong purifying selection (average ? = 0.0168), some subfamilies did experience
strong episodic positive selection during their evolution. Photolyases were lost
in higher animals that suggests natural selection apparently became weaker in the
late stage of evolutionary history. The evolutionary time estimates suggested
that plant and animal CRYs evolved in the Neoproterozoic Era (~1000-541 Mya),
which might be a result of adaptation to the major climate and global light
regime changes occurred in that period of the Earth's geological history.
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