Evolution and function of non-SMC subunits of SMC5/6 complex

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Authors

KOZÁKOVÁ Lucie BEDNÁŘOVÁ Kateřina HUDSON Jessica GUÉRINEAU Marc LEHMANN Alan PALEČEK Jan

Year of publication 2013
Type Conference abstract
Citation
Description Structural Maintenance of Chromosomes (SMC) proteins are highly conserved from bacteria to humans and play fundamental roles in chromosome dynamics, gene regulation and DNA repair. SMC1/3 (cohesin) complex is involved in sister chromatid cohesion, SMC2/4 (condensin) contributes to chromosome condensation and SMC5/6 complex is involved in several DNA repair pathways. SMC5/6 heterodimer associates with four non-SMC elements (Nse). The human Nse3 ortholog MAGEG1, founding member of MAGE (Melanoma Antigen Gene) protein family, interacts with both NSE1 (RING-finger containing protein) and NSE4 subunits. The NSE1-MAGEG1-NSE4 subcomplex bridges the head domains of Smc5-Smc6 heterodimer. In our work we have determined interacting domains of Nse3/MAGEG1 and Nse4/EID proteins. The conservation of interacting surface suggests their tight co-evolution. Functional analysis showed involvement of both protein families in transcription regulation and uncovered one possible function of enigmatic MAGE proteins.
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