title: Are there specific readers of oxidized 5-methylcytosine bases?
abstract: 5-methylcytosine (5mC) was long thought to be the only enzymatically created modified DNA base in mammalian cells. The discovery of 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine as reaction products of the TET family 5mC oxidases has prompted extensive searches for proteins that specifically bind to these oxidized bases. However, only a few of such "reader" proteins have been identified and verified so far. In this review, we discuss potential biological functions of oxidized 5mC as well as the role the presumed reader proteins may play in interpreting the genomic signals of 5mC oxidation products.
authors.affiliation: Department of Biochemistry, University of California Riverside, Riverside, CA, USA. jikui.song@ucr.edu.
authors.forename: Jikui
authors.initials: J
authors.lastname: Song
authors.affiliation: Center for Epigenetics, Van Andel Research Institute, Grand Rapids, MI, USA. gerd.pfeifer@vai.org.
authors.forename: Gerd P
authors.initials: GP
authors.lastname: Pfeifer
mesh_terms: D044503:5-Methylcytosine / Q000031:analogs & derivatives / Q000378:metabolism; D000818:Animals; D003596:Cytosine / Q000031:analogs & derivatives / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans
chemical_list: C560974:5-carboxylcytosine; C560973:5-formylcytosine; D004268:DNA-Binding Proteins; C011865:5-hydroxymethylcytosine; D044503:5-Methylcytosine; D003596:Cytosine; D004247:DNA
keywords: 5-carboxylcytosine; 5-formylcytosine; 5-hydroxymethylcytosine; 5-methylcytosine; TET proteins; chromatin readers