| First Author | Robertson AB | Year | 2014 |
| Journal | Nucleic Acids Res | Volume | 42 |
| Issue | 21 | Pages | 13280-93 |
| PubMed ID | 25355512 | Mgi Jnum | J:218272 |
| Mgi Id | MGI:5617102 | Doi | 10.1093/nar/gku1032 |
| Citation | Robertson AB, et al. (2014) Endonuclease G preferentially cleaves 5-hydroxymethylcytosine-modified DNA creating a substrate for recombination. Nucleic Acids Res 42(21):13280-93 |
| abstractText | 5-hydroxymethylcytosine (5hmC) has been suggested to be involved in various nucleic acid transactions and cellular processes, including transcriptional regulation, demethylation of 5-methylcytosine and stem cell pluripotency. We have identified an activity that preferentially catalyzes the cleavage of double-stranded 5hmC-modified DNA. Using biochemical methods we purified this activity from mouse liver extracts and demonstrate that the enzyme responsible for the cleavage of 5hmC-modified DNA is Endonuclease G (EndoG). We show that recombinant EndoG preferentially recognizes and cleaves a core sequence when one specific cytosine within that core sequence is hydroxymethylated. Additionally, we provide in vivo evidence that EndoG catalyzes the formation of double-stranded DNA breaks and that this cleavage is dependent upon the core sequence, EndoG and 5hmC. Finally, we demonstrate that the 5hmC modification can promote conservative recombination in an EndoG-dependent manner. |
