| First Author | Mistry H | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 375 |
| Issue | 3 | Pages | 321-5 |
| PubMed ID | 18692478 | Mgi Jnum | J:140323 |
| Mgi Id | MGI:3813377 | Doi | 10.1016/j.bbrc.2008.07.146 |
| Citation | Mistry H, et al. (2008) Interplay between Np95 and Eme1 in the DNA damage response. Biochem Biophys Res Commun 375(3):321-5 |
| abstractText | Mus81 (methyl methansulfonate UV sensitive clone 81) and Eme1 (essential meiotic endonuclease 1, also known as MMS4) form a heterodimeric endonuclease that is critical for genomic stability and the response to DNA crosslink damage and replication blockade. However, relatively little is known as to how this endonuclease is regulated following DNA damage. Here, we report mammalian Eme1 interacts with Np95, an E3 ubiquitin ligase that participates in chromatin modification, replication-linked epigenetic maintenance and the DNA damage response. Np95 and Eme1 co-localize on nuclear chromatin following exposure of cells to camptothecin, an agent that promotes the collapse of replication forks. The observed co localization following DNA damage was found to be dependent on an intact RING finger, the structural motif that encodes the E3 ubiquitin ligase activity of Np95. Taken together, these findings link Mus81-Eme1 with the replication-associated chromatin modifier functions of Np95 in the cellular response to DNA damage. |
