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further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome."}

{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T8256","span":{"begin":59,"end":67},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8257","span":{"begin":94,"end":99},"obj":"NCBITaxon_EXT:yeast"},{"id":"T8258","span":{"begin":140,"end":148},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8259","span":{"begin":154,"end":158},"obj":"CHEMINF_GO_EXT:chemical_binding_or_bond_formation"},{"id":"T8260","span":{"begin":166,"end":171},"obj":"NCBITaxon:9606"},{"id":"T8261","span":{"begin":177,"end":185},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8262","span":{"begin":228,"end":233},"obj":"UBERON:0000955"},{"id":"T8263","span":{"begin":298,"end":305},"obj":"PR_EXT:000043452"},{"id":"T8264","span":{"begin":298,"end":305},"obj":"CHEBI:15358"},{"id":"T8265","span":{"begin":298,"end":323},"obj":"GO_EXT:0004402"},{"id":"T8266","span":{"begin":324,"end":331},"obj":"PR_EXT:Q92830"},{"id":"T8267","span":{"begin":364,"end":371},"obj":"SO_EXT:0001060"},{"id":"T8268","span":{"begin":375,"end":383},"obj":"CHEBI:26537"},{"id":"T8269","span":{"begin":375,"end":394},"obj":"GO_EXT:0004886"},{"id":"T8270","span":{"begin":375,"end":396},"obj":"PR_EXT:000014373"},{"id":"T8271","span":{"begin":402,"end":409},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8272","span":{"begin":439,"end":445},"obj":"SO_EXT:0000417"},{"id":"T8273","span":{"begin":449,"end":454},"obj":"PR_EXT:000016007"},{"id":"T8274","span":{"begin":518,"end":521},"obj":"GO_PR_EXT:glutathione_S_transferase"},{"id":"T8275","span":{"begin":557,"end":561},"obj":"PR_EXT:000014373"},{"id":"T8276","span":{"begin":596,"end":603},"obj":"GO:0005634"},{"id":"T8277","span":{"begin":604,"end":611},"obj":"CHEBI_GO_EXT:hormone"},{"id":"T8278","span":{"begin":612,"end":620},"obj":"GO_EXT:0004872"},{"id":"T8279","span":{"begin":622,"end":628},"obj":"PR_EXT:Q965W2"},{"id":"T8280","span":{"begin":635,"end":645},"obj":"NCBITaxon:6239"},{"id":"T8281","span":{"begin":678,"end":685},"obj":"CHEMINF_GO_EXT:chemical_binding_or_bond_formation"},{"id":"T8282","span":{"begin":686,"end":693},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8283","span":{"begin":694,"end":699},"obj":"PR_EXT:P34427"},{"id":"T8284","span":{"begin":736,"end":746},"obj":"NCBITaxon:33317"},{"id":"T8285","span":{"begin":776,"end":783},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8286","span":{"begin":846,"end":855},"obj":"NCBITaxon:1"},{"id":"T8287","span":{"begin":923,"end":931},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8288","span":{"begin":1045,"end":1052},"obj":"SO_EXT:0000417"},{"id":"T8289","span":{"begin":1057,"end":1068},"obj":"SO_EXT:sequence_duplication_entity_or_process"},{"id":"T8290","span":{"begin":1076,"end":1084},"obj":"NCBITaxon:7711"},{"id":"T8291","span":{"begin":1145,"end":1155},"obj":"NCBITaxon:7742"},{"id":"T8292","span":{"begin":1161,"end":1168},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8293","span":{"begin":1178,"end":1193},"obj":"GO_EXT:transcription"},{"id":"T8294","span":{"begin":1178,"end":1205},"obj":"GO_EXT:0003713"},{"id":"T8295","span":{"begin":1251,"end":1255},"obj":"PR_EXT:000004303"},{"id":"T8296","span":{"begin":1256,"end":1269},"obj":"GO_EXT:transcription"},{"id":"T8297","span":{"begin":1256,"end":1276},"obj":"GO_EXT:transcription_factor"},{"id":"T8298","span":{"begin":1313,"end":1325},"obj":"NCBITaxon:33511"},{"id":"T8299","span":{"begin":1339,"end":1345},"obj":"SO_EXT:sequence_repeat_unit_or_region"},{"id":"T8300","span":{"begin":1361,"end":1366},"obj":"PR_EXT:000017527"},{"id":"T8301","span":{"begin":1404,"end":1409},"obj":"NCBITaxon:9606"},{"id":"T8302","span":{"begin":1410,"end":1446},"obj":"GO:0016514"},{"id":"T8303","span":{"begin":1418,"end":1438},"obj":"GO:0006338"},{"id":"T8304","span":{"begin":1475,"end":1490},"obj":"NCBITaxon:7227"},{"id":"T8305","span":{"begin":1491,"end":1500},"obj":"SO_EXT:0000853"},{"id":"T8306","span":{"begin":1504,"end":1509},"obj":"PR_EXT:000017527"},{"id":"T8307","span":{"begin":1668,"end":1681},"obj":"SO_EXT:0000657"},{"id":"T8308","span":{"begin":1689,"end":1699},"obj":"NCBITaxon:7215"},{"id":"T8309","span":{"begin":1705,"end":1712},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8310","span":{"begin":1745,"end":1755},"obj":"NCBITaxon:7742"},{"id":"T8311","span":{"begin":1819,"end":1834},"obj":"GO_EXT:transcription"},{"id":"T8312","span":{"begin":1835,"end":1845},"obj":"GO:0065007"},{"id":"T8313","span":{"begin":1846,"end":1855},"obj":"GO:0032991"},{"id":"T8314","span":{"begin":1866,"end":1874},"obj":"GO:0030674"},{"id":"T8315","span":{"begin":1875,"end":1885},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8316","span":{"begin":1932,"end":1939},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8317","span":{"begin":1969,"end":1975},"obj":"SO_EXT:0000417"},{"id":"T8318","span":{"begin":2032,"end":2043},"obj":"NCBITaxon:33317"},{"id":"T8319","span":{"begin":2048,"end":2061},"obj":"NCBITaxon:33511"},{"id":"T8320","span":{"begin":2111,"end":2119},"obj":"GO:0030674"},{"id":"T8321","span":{"begin":2120,"end":2127},"obj":"CHEBI_PR_EXT:protein"},{"id":"T8322","span":{"begin":2142,"end":2148},"obj":"PR_EXT:Q27365"},{"id":"T8323","span":{"beg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further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T8139","span":{"begin":166,"end":171},"obj":"NCBITaxon:9606"},{"id":"T8140","span":{"begin":228,"end":233},"obj":"UBERON:0000955"},{"id":"T8141","span":{"begin":298,"end":305},"obj":"PR:000043452"},{"id":"T8142","span":{"begin":298,"end":305},"obj":"CHEBI:15358"},{"id":"T8143","span":{"begin":324,"end":331},"obj":"PR:Q92830"},{"id":"T8144","span":{"begin":364,"end":371},"obj":"SO:0001060"},{"id":"T8145","span":{"begin":375,"end":383},"obj":"CHEBI:26537"},{"id":"T8146","span":{"begin":375,"end":396},"obj":"PR:000014373"},{"id":"T8147","span":{"begin":439,"end":445},"obj":"SO:0000417"},{"id":"T8148","span":{"begin":449,"end":454},"obj":"PR:000016007"},{"id":"T8149","span":{"begin":557,"end":561},"obj":"PR:000014373"},{"id":"T8150","span":{"begin":596,"end":603},"obj":"GO:0005634"},{"id":"T8151","span":{"begin":622,"end":628},"obj":"PR:Q965W2"},{"id":"T8152","span":{"begin":635,"end":645},"obj":"NCBITaxon:6239"},{"id":"T8153","span":{"begin":694,"end":699},"obj":"PR:P34427"},{"id":"T8154","span":{"begin":736,"end":746},"obj":"NCBITaxon:33317"},{"id":"T8155","span":{"begin":846,"end":855},"obj":"NCBITaxon:1"},{"id":"T8156","span":{"begin":1045,"end":1052},"obj":"SO:0000417"},{"id":"T8157","span":{"begin":1076,"end":1084},"obj":"NCBITaxon:7711"},{"id":"T8158","span":{"begin":1145,"end":1155},"obj":"NCBITaxon:7742"},{"id":"T8159","span":{"begin":1251,"end":1255},"obj":"PR:000004303"},{"id":"T8160","span":{"begin":1313,"end":1325},"obj":"NCBITaxon:33511"},{"id":"T8161","span":{"begin":1361,"end":1366},"obj":"PR:000017527"},{"id":"T8162","span":{"begin":1404,"end":1409},"obj":"NCBITaxon:9606"},{"id":"T8163","span":{"begin":1410,"end":1446},"obj":"GO:0016514"},{"id":"T8164","span":{"begin":1418,"end":1438},"obj":"GO:0006338"},{"id":"T8165","span":{"begin":1475,"end":1490},"obj":"NCBITaxon:7227"},{"id":"T8166","span":{"begin":1491,"end":1500},"obj":"SO:0000853"},{"id":"T8167","span":{"begin":1504,"end":1509},"obj":"PR:000017527"},{"id":"T8168","span":{"begin":1668,"end":1681},"obj":"SO:0000657"},{"id":"T8169","span":{"begin":1689,"end":1699},"obj":"NCBITaxon:7215"},{"id":"T8170","span":{"begin":1745,"end":1755},"obj":"NCBITaxon:7742"},{"id":"T8171","span":{"begin":1835,"end":1845},"obj":"GO:0065007"},{"id":"T8172","span":{"begin":1846,"end":1855},"obj":"GO:0032991"},{"id":"T8173","span":{"begin":1866,"end":1874},"obj":"GO:0030674"},{"id":"T8174","span":{"begin":1969,"end":1975},"obj":"SO:0000417"},{"id":"T8175","span":{"begin":2032,"end":2043},"obj":"NCBITaxon:33317"},{"id":"T8176","span":{"begin":2048,"end":2061},"obj":"NCBITaxon:33511"},{"id":"T8177","span":{"begin":2111,"end":2119},"obj":"GO:0030674"},{"id":"T8178","span":{"begin":2142,"end":2148},"obj":"PR:Q27365"},{"id":"T8179","span":{"begin":2150,"end":2155},"obj":"PR:P34427"},{"id":"T8180","span":{"begin":2159,"end":2164},"obj":"PR:000009822"},{"id":"T8181","span":{"begin":2204,"end":2210},"obj":"PR:Q27365"},{"id":"T8182","span":{"begin":2212,"end":2217},"obj":"PR:P34427"},{"id":"T8183","span":{"begin":2222,"end":2227},"obj":"PR:000009822"},{"id":"T8184","span":{"begin":2228,"end":2238},"obj":"SO:0000853"},{"id":"T8185","span":{"begin":2249,"end":2258},"obj":"NCBITaxon:1"},{"id":"T8186","span":{"begin":2342,"end":2349},"obj":"GO:0032991"},{"id":"T8187","span":{"begin":2381,"end":2387},"obj":"SO:0001026"}],"text":"To further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome."}

{"project":"2_test","denotations":[{"id":"15207008-12620397-9666058","span":{"begin":187,"end":188},"obj":"12620397"},{"id":"15207008-14767476-9666059","span":{"begin":189,"end":191},"obj":"14767476"},{"id":"15207008-14767476-9666060","span":{"begin":333,"end":335},"obj":"14767476"},{"id":"15207008-11025203-9666061","span":{"begin":1278,"end":1279},"obj":"11025203"},{"id":"15207008-12620397-9666062","span":{"begin":1448,"end":1449},"obj":"12620397"},{"id":"15207008-11903063-9666063","span":{"begin":1450,"end":1452},"obj":"11903063"}],"text":"To further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome."}