TY - JOUR
AU - Spada, Fabio
AB - In mammalian genomes a sixth base, 5-hydroxymethylcytosine (hmC), is generated by enzymatic oxidation of 5-methylcytosine (mC). This discovery has raised fundamental questions about the functional relevance of hmC in mammalian genomes. Due to their very similar chemical structure, discrimination of the rare hmC against the far more abundant mC is technically challenging and to date no methods for direct sequencing of hmC have been reported. Here, we report on a purified recombinant endonuclease, PvuRts1I, which selectively cleaves hmC-containing sequences. We determined the consensus cleavage site of PvuRts1I as hmCN1112/N910G and show first data on its potential to interrogate hmC patterns in mammalian genomes.
TI - Characterization of PvuRts1I endonuclease as a tool to investigate genomic 5hydroxymethylcytosine
JF - Nucleic Acids Research
DO - 10.1093/nar/gkr118
DA - 2011-07-04
UR - https://www.deepdyve.com/lp/oxford-university-press/characterization-of-pvurts1i-endonuclease-as-a-tool-to-investigate-FN0sgD1b5t
SP - 5149
EP - 5156
VL - 39
IS - 12
DP - DeepDyve
ER -