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Are there specific readers of oxidized 5‐methylcytosine bases?
Author(s) -
Song Jikui,
Pfeifer Gerd P.
Publication year - 2016
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201600126
Subject(s) - 5 methylcytosine , 5 hydroxymethylcytosine , cytosine , dna , computational biology , biology , chemistry , biochemistry , dna methylation , gene , gene expression
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.