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@proceedings{964680,
author = {Bednářová, Kateřina and Hudson, Jessica and Kozáková, Lucie and Guérineau, Marc and Marek, Jaromír and Lehmann, Alan R. and Paleček, Jan and Kozáková, Lucie and Guérineau, Marc and Marek, Jaromír and Lehman, Alan R. and Paleček, Jan},
booktitle = {XIV. Setkání biochemiků a molekulárních biologů},
keywords = {SMC5-6 complex; Nse3/MAGE proteins; Nse4/EID proteins},
language = {eng},
title = {The NSE3/MAGE interactions with NSE4/EID proteins are evolutionarily conserved},
year = {2010}
}
TY - CONF
ID - 964680
AU - Bednářová, Kateřina - Hudson, Jessica - Kozáková, Lucie - Guérineau, Marc - Marek, Jaromír - Lehmann, Alan R. - Paleček, Jan - Kozáková, Lucie - Guérineau, Marc - Marek, Jaromír - Lehman, Alan R. - Paleček, Jan
PY - 2010
TI - The NSE3/MAGE interactions with NSE4/EID proteins are evolutionarily conserved
KW - SMC5-6 complex
KW - Nse3/MAGE proteins
KW - Nse4/EID proteins
N2 - 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.
ER -
BEDNÁŘOVÁ, Kateřina, Jessica HUDSON, Lucie KOZÁKOVÁ, Marc GUÉRINEAU, Jaromír MAREK, Alan R. LEHMANN and Jan PALEČEK. The NSE3/MAGE interactions with NSE4/EID proteins are evolutionarily conserved. In KOZÁKOVÁ, Lucie, Marc GUÉRINEAU, Jaromír MAREK, Alan R. LEHMAN and Jan PALEČEK. \textit{XIV. Setkání biochemiků a molekulárních biologů}. 2010.
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