@article{
 title = {Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3},
 type = {article},
 year = {2004},
 pages = {39789-39797},
 volume = {279},
 id = {8ae82118-628a-3d0f-85fb-40ef4ede1b72},
 created = {2023-01-10T01:46:07.273Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:46:07.273Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {Classic zinc finger domains (cZFs) consist of a β-hairpin followed by an α-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an α-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the α-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the α-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.},
 bibtype = {article},
 author = {Simpson, R.J.Y. and Lee, S.H.Y. and Bartle, N. and Sum, E.Y. and Visvader, J.E. and Matthews, J.M. and Mackay, J.P. and Crossley, M.},
 doi = {10.1074/jbc.M404130200},
 journal = {Journal of Biological Chemistry},
 number = {38}
}

{"_id":"fb29umv3dGh9fDvXN","bibbaseid":"simpson-lee-bartle-sum-visvader-matthews-mackay-crossley-classiczincfingerfromfriendofgatamediatesaninteractionwiththecoiledcoiloftransformingacidiccoiledcoil3-2004","author_short":["Simpson, R.","Lee, S.","Bartle, N.","Sum, E.","Visvader, J.","Matthews, J.","Mackay, J.","Crossley, M."],"bibdata":{"title":"Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3","type":"article","year":"2004","pages":"39789-39797","volume":"279","id":"8ae82118-628a-3d0f-85fb-40ef4ede1b72","created":"2023-01-10T01:46:07.273Z","file_attached":false,"profile_id":"a5a2ab6f-a8b5-3db6-97bc-618752ee4386","group_id":"bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2","last_modified":"2023-01-10T01:46:07.273Z","read":false,"starred":false,"authored":false,"confirmed":false,"hidden":false,"private_publication":false,"abstract":"Classic zinc finger domains (cZFs) consist of a β-hairpin followed by an α-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an α-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the α-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the α-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.","bibtype":"article","author":"Simpson, R.J.Y. and Lee, S.H.Y. and Bartle, N. and Sum, E.Y. and Visvader, J.E. and Matthews, J.M. and Mackay, J.P. and Crossley, M.","doi":"10.1074/jbc.M404130200","journal":"Journal of Biological Chemistry","number":"38","bibtex":"@article{\n title = {Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3},\n type = {article},\n year = {2004},\n pages = {39789-39797},\n volume = {279},\n id = {8ae82118-628a-3d0f-85fb-40ef4ede1b72},\n created = {2023-01-10T01:46:07.273Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:46:07.273Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {Classic zinc finger domains (cZFs) consist of a β-hairpin followed by an α-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an α-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the α-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the α-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.},\n bibtype = {article},\n author = {Simpson, R.J.Y. and Lee, S.H.Y. and Bartle, N. and Sum, E.Y. and Visvader, J.E. and Matthews, J.M. and Mackay, J.P. and Crossley, M.},\n doi = {10.1074/jbc.M404130200},\n journal = {Journal of Biological Chemistry},\n number = {38}\n}","author_short":["Simpson, R.","Lee, S.","Bartle, N.","Sum, E.","Visvader, J.","Matthews, J.","Mackay, J.","Crossley, M."],"biburl":"https://bibbase.org/service/mendeley/a5a2ab6f-a8b5-3db6-97bc-618752ee4386","bibbaseid":"simpson-lee-bartle-sum-visvader-matthews-mackay-crossley-classiczincfingerfromfriendofgatamediatesaninteractionwiththecoiledcoiloftransformingacidiccoiledcoil3-2004","role":"author","urls":{},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/service/mendeley/a5a2ab6f-a8b5-3db6-97bc-618752ee4386","dataSources":["Qyiuzjmxwb6Qg6BFv","ToyCPY2rxgiQ4m4by","rdWS9Da3o8ATA9vPu","ya2CyA73rpZseyrZ8","GHkD7mCKXmQCzS4W8","4BKYoCQJ3ndMcbbtH","2252seNhipfTmjEBQ"],"keywords":[],"search_terms":["classic","zinc","finger","friend","gata","mediates","interaction","coiled","coil","transforming","acidic","coiled","coil","simpson","lee","bartle","sum","visvader","matthews","mackay","crossley"],"title":"Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3","year":2004}