Are there specific readers of oxidized 5-methylcytosine bases?

Bioessays. 2016 Oct;38(10):1038-47. doi: 10.1002/bies.201600126. Epub 2016 Aug 2.

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.

Keywords: 5-carboxylcytosine; 5-formylcytosine; 5-hydroxymethylcytosine; 5-methylcytosine; TET proteins; chromatin readers.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5-Methylcytosine / analogs & derivatives
  • 5-Methylcytosine / metabolism
  • Animals
  • Cytosine / analogs & derivatives
  • Cytosine / metabolism
  • DNA / chemistry
  • DNA / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Humans

Substances

  • 5-carboxylcytosine
  • 5-formylcytosine
  • DNA-Binding Proteins
  • 5-hydroxymethylcytosine
  • 5-Methylcytosine
  • Cytosine
  • DNA