The Photolyase/Cryptochrome Family of Proteins as DNA Repair Enzymes and Transcriptional Repressors
İbrahim Halil Kavaklıa b c d e f✉, İbrahim Barışc f, Mehmet Tardub e, Şeref Güla d, Haşimcan Önera d, Sibel Cal‐Kayitmazbatirc f, Selma Buluta d, Darya Yarparvara d, Çağlar Berkelc f, Pınar Ustaoğluc f, Cihan Aydıng h
- aDepartment of Chemical and Biological Engineering Koc University Sariyer Istanbul Turkey
- bDepartment of Computational Science and Engineering Koc University Sariyer Istanbul Turkey
- cDepartment of Molecular Biology and Genetics Koc University Sariyer Istanbul Turkey
- dDepartment of Chemical and Biological Engineering, Koc University, Sariyer, Istanbul, Turkey
- eDepartment of Computational Science and Engineering, Koc University, Sariyer, Istanbul, Turkey
- fDepartment of Molecular Biology and Genetics, Koc University, Sariyer, Istanbul, Turkey
- gDepartment of Molecular Biology and Genetics Istanbul Medeniyet University Uskudar Istanbul
- hDepartment of Molecular Biology and Genetics, Istanbul Medeniyet University, Uskudar, Istanbul
- ✉Corresponding author
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Abstract
Light is a very important environmental factor that governs many cellular responses in organisms. As a consequence, organisms possess different kinds of light-sensing photoreceptors to regulate their physiological variables and adapt to a given habitat. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum. On the other hand, cryptochromes act as blue light circadian photoreceptors in plants and Drosophila to regulate growth and development. In mammals, cryptochromes have light-independent functions and are very important transcriptional regulators that act at the molecular level as negative transcriptional regulators of the circadian clock. In this review, we highlight current knowledge concerning the structural and functional relationships of CPF members.