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Recognition of 5-Hydroxymethylcytosine by the Uhrf1 SRA Domain

Open access
Frauer, Carina, Hoffmann, Thomas, Bultmann, Sebastian, Casa, Valentina, Cardoso, M. Cristina, Antes, Iris, Leonhardt, Heinrich·2011·PLoS ONE

Abstract

Recent discovery of 5-hydroxymethylcytosine (5hmC) in genomic DNA raises the question how this sixth base is recognized by cellular proteins. In contrast to the methyl-CpG binding domain (MBD) of MeCP2, we found that the SRA domain of Uhrf1, an essential factor in DNA maintenance methylation, binds 5hmC and 5-methylcytosine containing substrates with similar affinity. Based on the co-crystal structure, we performed molecular dynamics simulations of the SRA:DNA complex with the flipped cytosine base carrying either of these epigenetic modifications. Our data indicate that the SRA binding pocket can accommodate 5hmC and stabilizes the flipped base by hydrogen bond formation with the hydroxyl group.

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Metadata

Authors
Frauer, C., Hoffmann, T., Bultmann, S., Casa, V., Cardoso, M. C., Antes, I., & Leonhardt, H.
Venue
PLoS ONE
Published
2011-06-22
Volume
6
Issue
6
Pages
e21306
ISSN
1932-6203 (ISSN-L)
OpenAlex
W1989467586
Cited by
180
References
6
FWCI
10.58
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Recognition of 5-Hydroxymethylcytosine by the Uhrf1 SRA Domain. https://app.cochat.ai/papers/10.1371/journal.pone.0021306
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Frauer, C., Hoffmann, T., Bultmann, S., Casa, V., Cardoso, M. C., Antes, I., & Leonhardt, H. (2011). Recognition of 5-Hydroxymethylcytosine by the Uhrf1 SRA Domain. PLoS ONE. https://doi.org/10.1371/journal.pone.0021306

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