A Classic Zinc Finger from Friend of GATA Mediates an Interaction with the Coiled-coil of Transforming Acidic Coiled-coil 3. Simpson, R., J., Y., Yi Lee, S., H., Bartle, N., Sum, E., Y., Visvader, J., E., Matthews, J., M., Mackay, J., P., & Crossley, M. Journal of Biological Chemistry, 279(38):39789-39797, 9, 2004. ![A Classic Zinc Finger from Friend of GATA Mediates an Interaction with the Coiled-coil of Transforming Acidic Coiled-coil 3 [link]](https://bibbase.org/img/filetypes/link.svg "link")
Website doi abstract bibtex Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by an alpha-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 alpha-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 alpha-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the alpha-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.
@article{
title = {A 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},
websites = {http://www.ncbi.nlm.nih.gov/pubmed/15234987},
month = {9},
day = {17},
id = {5c9d3a6d-094f-32b9-82b5-a8e3f79b3a58},
created = {2020-10-01T06:20:29.182Z},
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last_modified = {2020-10-29T21:44:44.134Z},
read = {false},
starred = {false},
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confirmed = {true},
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citation_key = {Simpson2004},
source_type = {ARTICLE},
notes = {cited By 26},
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abstract = {Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by an alpha-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 alpha-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 alpha-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the alpha-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, Raina J. Y. and Yi Lee, Stella Hoi and Bartle, Natalie and Sum, Eleanor Y. and Visvader, Jane E. and Matthews, Jacqueline M. and Mackay, Joel P. and Crossley, Merlin},
doi = {10.1074/jbc.M404130200},
journal = {Journal of Biological Chemistry},
number = {38}
}
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