X-ray crystallography and NMR show that 5-formylcytosine does not change the global structure of DNA

The mechanism by which 5-formylcytosine (fC) is recognised by enzymes involved in epigenetic modification and reading of DNA is not known, and recently an unusual DNA structure (F-DNA) was proposed as the basis for enzyme recognition of clusters of fC. We used NMR and X-ray crystallography to compar...

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Bibliographic Details
Published inNature structural & molecular biology Vol. 24; no. 6; pp. 544 - 552
Main Authors Hardwick, Jack S, Ptchelkine, Denis, El-Sagheer, Afaf H, Tear, Ian, Singleton, Daniel, Phillips, Simon E V, Lane, Andrew N, Brown, Tom
Format Journal Article
LanguageEnglish
Published Nature Publishing Group 29.12.2017
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Summary:The mechanism by which 5-formylcytosine (fC) is recognised by enzymes involved in epigenetic modification and reading of DNA is not known, and recently an unusual DNA structure (F-DNA) was proposed as the basis for enzyme recognition of clusters of fC. We used NMR and X-ray crystallography to compare several modified DNA duplexes with the unmodified analogues and show that in the crystal state they all belong to the A-family, but in solution they are all members of the B-family. Contrary to the previous study, we find that 5-formylcytosine does not significantly affect the structure of DNA, though there are modest local differences at the modification sites. Hence, global conformation changes are unlikely to account for the recognition *
Bibliography:joint first authors
ISSN:1545-9993
1545-9985
DOI:10.1038/nsmb.3411