The NSE3/MAGE interactions with NSE4/EID proteins are  evolutionarily conserved

Zábrady,  Kateřina; Bozděchová,  Lucie; Hudson, Jessica; Guérineau,  Marc; Bozděchová,  Lucie; Marek,  Jaromír; Guérineau,  Marc; Lehman, Alan R.; Marek,  Jaromír; Paleček,  Jan; Lehmann, Alan R.; Paleček,  Jan

The NSE3/MAGE interactions with NSE4/EID proteins are evolutionarily conserved

Warning

This publication doesn't include Faculty of Economics and Administration. It includes Faculty of Science. Official publication website can be found on muni.cz.

Authors	BEDNÁŘOVÁ Kateřina KOZÁKOVÁ Lucie HUDSON Jessica GUÉRINEAU Marc KOZÁKOVÁ Lucie MAREK Jaromír GUÉRINEAU Marc LEHMAN Alan R. MAREK Jaromír PALEČEK Jan LEHMANN Alan R. PALEČEK Jan
Year of publication	2010
Type	Conference abstract
MU Faculty or unit	Faculty of Science
Citation
Description	Structural Maintenance of Chromosomes (SMC) complexes are involved in a wide range of cellular processes from cell division to gene regulation and DNA repair. In eukaryotes, three separate SMC protein complexes are conserved. Each contains a heterodimeric core of two SMC proteins interconnected by a kleisin subunit, together with from one to five more non-SMC elements (Nse). The complex containing SMC1 and SMC3, named cohesin, is responsible for sister chromatid cohesion during mitosis and meiosis. The condensin complex with SMC2 and SMC4 at its core is required for proper chromosome condensation and segregation during cell division. Both cohesin and condensin are also involved in gene regulation and DNA repair. The less well characterized SMC5/6 complex is involved in several DNA repair pathways. The SMC5/6 complex is composed of two subcomlexes SMC5-SMC6-Nse2 and Nse1-Nse3-Nse4. Nse3 shows sequence similarity to the Melanoma Antigen Gene (MAGE) family of proteins, which are overexpressed in certain types of cancers and whose function has been linked to cell cycle regulation, apoptosis and neuronal development. Using site-directed mutagenesis, protein-protein interaction analyses and modelling of the Schizosaccharomyces pombe Nse3 onto the crystal structure of the MAGEA4 protein, we have identified surface on the C-terminal domain of Nse3 that interacts with Nse4. The binding site for Nse4 is well conserved within the Nse3/MAGE superfamily of proteins. Nse4 is related to the EID (E1A-like inhibitor of differentiation) family of transcriptional repressors. We show that there is a relatively promiscuous interaction between members of the MAGE family and those of the EID family with some specificity. Our data suggest that the Nse3/MAGE-Nse4/EID interaction is evolutionarily conserved.
Related projects:	Molecular basis of cell and tissue regulations Molecular mechanisms of the cell proliferation and differentiation Charakterizace MAGE proteinů: kofaktory E3 ubiquitin ligáz?