Interactions between the Nse3 and Nse4 Components of the SMC5-6 Complex Identify Evolutionarily Conserved Interactions between MAGE and EID Families
| Authors | |
|---|---|
| Year of publication | 2011 |
| Type | Article in Periodical |
| Magazine / Source | PloS ONE |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0017270 |
| Doi | http://dx.doi.org/10.1371/journal.pone.0017270 |
| Field | Biochemistry |
| Keywords | SMC5-6 complex; Nse3/MAGE; Nse4/EID; genome stability; transcription regulation; evolution; placental mammals |
| Description | The SMC5-6 protein complex is involved in the cellular response to DNA damage. It is composed of 6 - 8 polypeptides, of which Nse1, Nse3 and Nse4 form a tight sub-complex. MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and Nse4 is related to the EID (E1A-like inhibitor of differentiation) family of transcriptional repressors. We have identified a conserved hydrophobic surface on the C-terminal domain of Nse3 that interacts with Nse4 and identified residues in its N-terminal domain that are essential for interaction with Nse1. We show that these interactions are conserved in the human orthologs. In an examination of the evolutionary conservation of the Nse3-Nse4 interactions, we find that most MAGE proteins can interact with at least one of the NSE4/EID proteins. |
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