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Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives

Spruijt, Cornelia G. ; Gnerlich, Felix ; Smits, Arne H. ; Pfaffeneder, Toni ; Jansen, Pascal W.T.C. ; Bauer, Christina ; Münzel, Martin ; Wagner, Mirko ; Müller, Markus ; Khan, Fariha ; Eberl, H. Christian ; Mensinga, Anneloes ; Brinkman, Arie B. ; Lephikov, Konstantin ; Müller, Udo ; Walter, Jörn ; Boelens, Rolf ; van Ingen, Hugo ; Leonhardt, Heinrich ; Carell, Thomas ; Vermeulen, Michiel

Cell, 2013-02, Vol.152 (5), p.1146-1159 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives
Autor: Spruijt, Cornelia G. ; Gnerlich, Felix ; Smits, Arne H. ; Pfaffeneder, Toni ; Jansen, Pascal W.T.C. ; Bauer, Christina ; Münzel, Martin ; Wagner, Mirko ; Müller, Markus ; Khan, Fariha ; Eberl, H. Christian ; Mensinga, Anneloes ; Brinkman, Arie B. ; Lephikov, Konstantin ; Müller, Udo ; Walter, Jörn ; Boelens, Rolf ; van Ingen, Hugo ; Leonhardt, Heinrich ; Carell, Thomas ; Vermeulen, Michiel
Assuntos: 5-Methylcytosine - analysis ; 5-Methylcytosine - metabolism ; adults ; Animals ; brain ; Brain - cytology ; Brain - metabolism ; cytosine ; Cytosine - analogs & derivatives ; Cytosine - analysis ; Cytosine - metabolism ; DNA ; DNA damage ; DNA Glycosylases - metabolism ; DNA Methylation ; DNA repair ; DNA-Binding Proteins - metabolism ; embryonic stem cells ; Embryonic Stem Cells - metabolism ; Mass Spectrometry ; Mice ; Oxidation-Reduction ; proteins ; proteomics ; Proto-Oncogene Proteins - metabolism ; Regulatory Factor X Transcription Factors ; Stem Cells - metabolism ; transcription factors ; Transcription Factors - metabolism ; Ubiquitin-Protein Ligases - metabolism
É parte de: Cell, 2013-02, Vol.152 (5), p.1146-1159
Notas: http://dx.doi.org/10.1016/j.cell.2013.02.004
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Descrição: 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. [Display omitted] ► Identification of readers for 5-(hydroxy)methylcytosine in (differentiated) mESCs ► mC and hmC readers are highly dynamic during development and show limited overlap ► Oxidized derivatives of mC recruit DNA repair proteins in mESCs ► Uhrf2 stimulates the activity of the Tet1 enzyme Spruijt et al. identified protein binding partners of 5-methylcytosine and its oxidative derivatives. These dynamic and specific readers suggest a role for these bases in active DNA demethylation and a DNA demethylation-independent function.
Editor: United States: Elsevier Inc
Idioma: Inglês

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Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives

United States: Elsevier Inc

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