{"data":{"id":"10.6084/m9.figshare.1289848","type":"dois","attributes":{"doi":"10.6084/m9.figshare.1289848","prefix":"10.6084","suffix":"m9.figshare.1289848","identifiers":[],"alternateIdentifiers":[],"creators":[{"name":"Kozakova, Lucie","nameType":"Personal","givenName":"Lucie","familyName":"Kozakova","affiliation":[],"nameIdentifiers":[]},{"name":"Vondrova, Lucie","nameType":"Personal","givenName":"Lucie","familyName":"Vondrova","affiliation":[],"nameIdentifiers":[]},{"name":"Stejskal, Karel","nameType":"Personal","givenName":"Karel","familyName":"Stejskal","affiliation":[],"nameIdentifiers":[]},{"name":"Charalabous, Panagoula","nameType":"Personal","givenName":"Panagoula","familyName":"Charalabous","affiliation":[],"nameIdentifiers":[]},{"name":"Kolesar, Peter","nameType":"Personal","givenName":"Peter","familyName":"Kolesar","affiliation":[],"nameIdentifiers":[]},{"name":"Lehmann, Alan R","nameType":"Personal","givenName":"Alan R","familyName":"Lehmann","affiliation":[],"nameIdentifiers":[]},{"name":"Uldrijan, Stjepan","nameType":"Personal","givenName":"Stjepan","familyName":"Uldrijan","affiliation":[],"nameIdentifiers":[]},{"name":"Sanderson, Christopher M","nameType":"Personal","givenName":"Christopher M","familyName":"Sanderson","affiliation":[],"nameIdentifiers":[]},{"name":"Zbynek Zdrahal","affiliation":[],"nameIdentifiers":[]},{"name":"Palecek, Jan J","nameType":"Personal","givenName":"Jan J","familyName":"Palecek","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex"}],"publisher":"Taylor \u0026 Francis","container":{},"publicationYear":2015,"subjects":[{"subject":"Biophysics"},{"subject":"Biochemistry"},{"subject":"Cell Biology"},{"subject":"Genetics"},{"subject":"FOS: Biological sciences","schemeUri":"http://www.oecd.org/science/inno/38235147.pdf","subjectScheme":"Fields of Science and Technology (FOS)"},{"subject":"FOS: Biological sciences","subjectScheme":"Fields of Science and Technology (FOS)"},{"subject":"Molecular Biology"},{"subject":"Biotechnology"},{"subject":"Evolutionary Biology"},{"subject":"Immunology"},{"subject":"FOS: Clinical medicine","schemeUri":"http://www.oecd.org/science/inno/38235147.pdf","subjectScheme":"Fields of Science and Technology (FOS)"},{"subject":"FOS: Clinical medicine","subjectScheme":"Fields of Science and Technology (FOS)"},{"subject":"Developmental Biology"},{"subject":"Cancer"}],"contributors":[],"dates":[{"date":"2015-01-15","dateType":"Created"},{"date":"2018-08-31","dateType":"Updated"},{"date":"2015","dateType":"Issued"}],"language":null,"types":{"ris":"DATA","bibtex":"misc","citeproc":"dataset","schemaOrg":"Dataset","resourceType":"Dataset","resourceTypeGeneral":"Dataset"},"relatedIdentifiers":[{"relationType":"IsSupplementTo","relatedIdentifier":"10.1080/15384101.2014.1000112","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":["43999082 Bytes"],"formats":[],"version":null,"rightsList":[{"rights":"Creative Commons Attribution 4.0 International","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rightsIdentifier":"cc-by-4.0","rightsIdentifierScheme":"SPDX"}],"descriptions":[{"description":"The MAGE (Melanoma-associated antigen) protein family members are structurally related to each other by a MAGE-homology domain comprised of 2 winged helix motifs WH/A and WH/B. This family specifically evolved in placental mammals although single homologs designated NSE3 (non-SMC element) exist in most eukaryotes. NSE3, together with its partner proteins NSE1 and NSE4 form a tight subcomplex of the structural maintenance of chromosomes SMC5–6 complex. Previously, we showed that interactions of the WH/B motif of the MAGE proteins with their NSE4/EID partners are evolutionarily conserved (including the MAGEA1-NSE4 interaction). In contrast, the interaction of the WH/A motif of NSE3 with NSE1 diverged in the MAGE paralogs. We hypothesized that the MAGE paralogs acquired new RING-finger-containing partners through their evolution and form MAGE complexes reminiscent of NSE1-NSE3-NSE4 trimers. In this work, we employed the yeast 2-hybrid system to screen a human RING-finger protein library against several MAGE baits. We identified a number of potential MAGE-RING interactions and confirmed several of them (MDM4, PCGF6, RNF166, TRAF6, TRIM8, TRIM31, TRIM41) in co-immunoprecipitation experiments. Among these MAGE-RING pairs, we chose to examine MAGEA1-TRIM31 in detail and showed that both WH/A and WH/B motifs of MAGEA1 bind to the coiled-coil domain of TRIM31 and that MAGEA1 interaction stimulates TRIM31 ubiquitin-ligase activity. In addition, TRIM31 directly binds to NSE4, suggesting the existence of a TRIM31-MAGEA1-NSE4 complex reminiscent of the NSE1-NSE3-NSE4 trimer. These results suggest that MAGEA1 functions as a co-factor of TRIM31 ubiquitin-ligase and that the TRIM31-MAGEA1-NSE4 complex may have evolved from an ancestral NSE1-NSE3-NSE4 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