@ARTICLE{Simpson200439789,
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.},
title={Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3},
journal={Journal of Biological Chemistry},
year={2004},
volume={279},
number={38},
pages={39789-39797},
doi={10.1074/jbc.M404130200},
note={cited By 28},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-4544366535&doi=10.1074%2fjbc.M404130200&partnerID=40&md5=0f131222a132dcba70daed2a4487b34a},
affiliation={Sch. of Molec. and Microbial Biosci., University of Sydney, Sydney, NSW 2006, Australia; Walter/Eliza Hall Inst. of Med. Res., Bone Marrow Research Laboratories, Royal Melbourne Hospital, 1G Royal Parade, Parkville, Vic. 3050, Australia},
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.},
keywords={Derivatives;  DNA;  Surface phenomena;  Zinc, Classic zinc finger domains;  Mutational mapping;  Protein domains;  Tandem arrays, Proteins, cell protein;  friend of GATA transcription factor;  transcription factor;  transforming acidic coiled coil 3 protein;  unclassified drug, alpha helix;  article;  carboxy terminal sequence;  centrosome;  controlled study;  DNA binding;  gene mapping;  in vitro study;  nonhuman;  priority journal;  protein analysis;  protein domain;  protein engineering;  protein function;  protein protein interaction;  protein structure;  solubility;  structure analysis;  zinc finger motif, Amino Acid Sequence;  Animals;  Binding Sites;  Carrier Proteins;  Cells, Cultured;  Dimerization;  Fetal Proteins;  Humans;  Mice;  Molecular Sequence Data;  Nuclear Proteins;  Protein Structure, Quaternary;  Protein Structure, Secondary;  Protein Structure, Tertiary;  Solubility;  Transcription Factors;  Zinc Fingers},
correspondence_address1={Mackay, J.P.; Sch. of Molec. and Microbial Biosci., , Sydney, NSW 2006, Australia; email: j.mackay@mmb.usyd.edu.au},
issn={00219258},
coden={JBCHA},
pubmed_id={15234987},
language={English},
abbrev_source_title={J. Biol. Chem.},
document_type={Article},
source={Scopus},
}

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Res., Bone Marrow Research Laboratories, Royal Melbourne Hospital, 1G Royal Parade, Parkville, Vic. 3050, Australia","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.","keywords":"Derivatives; DNA; Surface phenomena; Zinc, Classic zinc finger domains; Mutational mapping; Protein domains; Tandem arrays, Proteins, cell protein; friend of GATA transcription factor; transcription factor; transforming acidic coiled coil 3 protein; unclassified drug, alpha helix; article; carboxy terminal sequence; centrosome; controlled study; DNA binding; gene mapping; in vitro study; nonhuman; priority journal; protein analysis; protein domain; protein engineering; protein function; protein protein interaction; protein structure; solubility; structure analysis; zinc finger motif, Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Cells, Cultured; Dimerization; Fetal Proteins; Humans; Mice; Molecular Sequence Data; Nuclear Proteins; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Solubility; Transcription Factors; Zinc Fingers","correspondence_address1":"Mackay, J.P.; Sch. of Molec. and Microbial Biosci., , Sydney, NSW 2006, Australia; email: j.mackay@mmb.usyd.edu.au","issn":"00219258","coden":"JBCHA","pubmed_id":"15234987","language":"English","abbrev_source_title":"J. Biol. Chem.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Simpson200439789,\nauthor={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.},\ntitle={Classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3},\njournal={Journal of Biological Chemistry},\nyear={2004},\nvolume={279},\nnumber={38},\npages={39789-39797},\ndoi={10.1074/jbc.M404130200},\nnote={cited By 28},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-4544366535&doi=10.1074%2fjbc.M404130200&partnerID=40&md5=0f131222a132dcba70daed2a4487b34a},\naffiliation={Sch. of Molec. and Microbial Biosci., University of Sydney, Sydney, NSW 2006, Australia; Walter/Eliza Hall Inst. of Med. Res., Bone Marrow Research Laboratories, Royal Melbourne Hospital, 1G Royal Parade, Parkville, Vic. 3050, Australia},\nabstract={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. 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Chem.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n","author_short":["Simpson, R.","Lee, S.","Bartle, N.","Sum, E.","Visvader, J.","Matthews, J.","Mackay, J.","Crossley, M."],"key":"Simpson200439789","id":"Simpson200439789","bibbaseid":"simpson-lee-bartle-sum-visvader-matthews-mackay-crossley-classiczincfingerfromfriendofgatamediatesaninteractionwiththecoiledcoiloftransformingacidiccoiledcoil3-2004","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4544366535&doi=10.1074%2fjbc.M404130200&partnerID=40&md5=0f131222a132dcba70daed2a4487b34a"},"keyword":["Derivatives; DNA; Surface phenomena; Zinc","Classic zinc finger domains; Mutational mapping; Protein domains; Tandem arrays","Proteins","cell protein; friend of GATA transcription factor; transcription factor; transforming acidic coiled coil 3 protein; unclassified drug","alpha helix; article; carboxy terminal sequence; centrosome; controlled study; DNA binding; gene mapping; in vitro study; nonhuman; priority journal; protein analysis; protein domain; protein engineering; protein function; protein protein interaction; protein structure; solubility; structure analysis; zinc finger motif","Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Cells","Cultured; Dimerization; Fetal Proteins; Humans; Mice; Molecular Sequence Data; Nuclear Proteins; Protein Structure","Quaternary; Protein Structure","Secondary; Protein Structure","Tertiary; Solubility; Transcription Factors; Zinc Fingers"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://mackaymatthewslab.org/documents/mackay.bib","dataSources":["Qyiuzjmxwb6Qg6BFv","ToyCPY2rxgiQ4m4by","rdWS9Da3o8ATA9vPu","ya2CyA73rpZseyrZ8","GHkD7mCKXmQCzS4W8","4BKYoCQJ3ndMcbbtH"],"keywords":["derivatives; dna; surface phenomena; zinc","classic zinc finger domains; mutational mapping; protein domains; tandem arrays","proteins","cell protein; friend of gata transcription factor; transcription factor; transforming acidic coiled coil 3 protein; unclassified drug","alpha helix; article; carboxy terminal sequence; centrosome; controlled study; dna binding; gene mapping; in vitro study; nonhuman; priority journal; protein analysis; protein domain; protein engineering; protein function; protein protein interaction; protein structure; solubility; structure analysis; zinc finger motif","amino acid sequence; animals; binding sites; carrier proteins; cells","cultured; dimerization; fetal proteins; humans; mice; molecular sequence data; nuclear proteins; protein structure","quaternary; protein structure","secondary; protein structure","tertiary; solubility; transcription factors; zinc fingers"],"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}