Journal
MOLECULAR BIOLOGY AND EVOLUTION
Volume 38, Issue 10, Pages 4505-4519Publisher
OXFORD UNIV PRESS
DOI: 10.1093/molbev/msab191
Keywords
photolyase; cryptochrome; cyclobutane pyrimidine dimer; iron-sulfur cluster; phylogenetic analysis
Funding
- National Natural Science Foundation of China [31971199]
- Natural Science Foundation of Anhui Province [1808085MH272]
- Young Backbone Talents Fund Project of Wannan Medical College (2019)
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UV irradiation leads to the formation of CPDs and 6-4 photoproducts in DNA, which can be repaired by CPD photolyases and 6-4 photolyases. A novel class of short photolyase-like proteins, identified through phylogenetic analyses, have high similarity to CPD photolyases and may be the ancestors of the cryptochrome/photolyase family.
UV irradiation induces the formation of cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts in DNA. These two types of lesions can be directly photorepaired by CPD photolyases and 6-4 photolyases, respectively. Recently, a new class of 6-4 photolyases named iron-sulfur bacterial cryptochromes and photolyases (FeS-BCPs) were found, which were considered as the ancestors of all photolyases and their homologs-cryptochromes. However, a controversy exists regarding 6-4 photoproducts only constituting similar to 10-30% of the total UV-induced lesions that primordial organisms would hardly survive without a CPD repair enzyme. By extensive phylogenetic analyses, we identified a novel class of proteins, all from eubacteria. They have relatively high similarity to class I/III CPD photolyases, especially in the putative substrate-binding and FAD-binding regions. However, these proteins are shorter, and they lack the N-terminal alpha/beta domain of normal photolyases. Therefore, we named them short photolyase-like. Nevertheless, similar to FeS-BCPs, some of short photolyase-likes also contain four conserved cysteines, which may also coordinate an iron-sulfur cluster as FeS-BCPs. A member from Rhodococcus fascians was cloned and expressed. It was demonstrated that the protein contains a FAD cofactor and an iron-sulfur cluster, and has CPD repair activity. It was speculated that this novel class of photolyases may be the real ancestors of the cryptochrome/photolyase family.
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