A topologically distinct class of photolyases specific for UV lesions within single-stranded DNA

Abstract Photolyases are ubiquitously occurring flavoproteins for catalyzing photo repair of UV-induced DNA damages. All photolyases described so far have a bilobal architecture with a C-terminal domain comprising flavin adenine dinucleotide (FAD) as catalytic cofactor and an N-terminal domain capab...

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Published inNucleic acids research Vol. 48; no. 22; pp. 12845 - 12857
Main Authors Emmerich, Hans-Joachim, Saft, Martin, Schneider, Leonie, Kock, Dennis, Batschauer, Alfred, Essen, Lars-Oliver
Format Journal Article
LanguageEnglish
Published England Oxford University Press 16.12.2020
Subjects
Amino Acid Sequence - genetics
Catalytic Domain - genetics
Catalytic Domain - radiation effects
Cryptochromes - genetics
Deoxyribodipyrimidine Photo-Lyase - genetics
Deoxyribodipyrimidine Photo-Lyase - radiation effects
DNA Damage - radiation effects
DNA Repair - radiation effects
DNA, Single-Stranded - genetics
DNA, Single-Stranded - radiation effects
Methylobacterium - genetics
Nucleic Acid Enzymes
Pyrimidine Dimers - genetics
Pyrimidine Dimers - radiation effects
Rhodobacteraceae - genetics
Ultraviolet Rays
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Summary:Abstract Photolyases are ubiquitously occurring flavoproteins for catalyzing photo repair of UV-induced DNA damages. All photolyases described so far have a bilobal architecture with a C-terminal domain comprising flavin adenine dinucleotide (FAD) as catalytic cofactor and an N-terminal domain capable of harboring an additional antenna chromophore. Using sequence-similarity network analysis we discovered a novel subgroup of the photolyase/cryptochrome superfamily (PCSf), the NewPHLs. NewPHL occur in bacteria and have an inverted topology with an N-terminal catalytic domain and a C-terminal domain for sealing the FAD binding site from solvent access. By characterizing two NewPHL we show a photochemistry characteristic of other PCSf members as well as light-dependent repair of CPD lesions. Given their common specificity towards single-stranded DNA many bacterial species use NewPHL as a substitute for DASH-type photolyases. Given their simplified architecture and function we suggest that NewPHL are close to the evolutionary origin of the PCSf.
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The authors wish it to be known that, in their opinion, the first two authors should be regarded as Joint First Authors.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkaa1147