Journal
CELL
Volume 152, Issue 5, Pages 1146-1159Publisher
CELL PRESS
DOI: 10.1016/j.cell.2013.02.004
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Funding
- DFG Normalverfahren [CA275/8-4, SFB 749, SFB 646]
- Volkswagen Foundation
- Deutsche Forschungsgemeinschaft (DFG) [SFB 646, SPP 1463]
- Fonds der Chemischen Industrie
- International Research Support Initiative Program from the Higher Education Commission, Pakistan
- Dutch Science Foundation Chemical Sciences, NWO-CW
- DFG [WA1029/6, SPP1356]
- Netherlands Organization for Scientific Research (NWO-VIDI)
- ERC
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Tet proteins oxidize 5-methylcytosine (mC) to generate 5-hydroxymethyl (hmC), 5-formyl (fC), and 5-carboxylcytosine (caC). The exact function of these oxidative cytosine bases remains elusive. We applied quantitative mass-spectrometry-based proteomics to identify readers for mC and hmC in mouse embryonic stem cells (mESC), neuronal progenitor cells (NPC), and adult mouse brain tissue. Readers for these modifications are only partially overlapping, and some readers, such as Rfx proteins, display strong specificity. Interactions are dynamic during differentiation, as for example evidenced by the mESC-specific binding of Klf4 to mC and the NPC-specific binding of Uhrf2 to hmC, suggesting specific biological roles for mC and hmC. Oxidized derivatives of mC recruit distinct transcription regulators as well as a large number of DNA repair proteins in mouse ES cells, implicating the DNA damage response as a major player in active DNA demethylation.
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