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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Published in | Nature structural & molecular biology Vol. 24; no. 6; pp. 544 - 552 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Nature Publishing Group
29.12.2017
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Subjects | |
Online Access | Get full text |
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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 * |
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Bibliography: | joint first authors |
ISSN: | 1545-9993 1545-9985 |
DOI: | 10.1038/nsmb.3411 |