A classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3
- Author(s)
- Simpson, RJY; Lee, SHY; Bartle, N; Sum, EY; Visvader, JE; Matthews, JM; Mackay, JP; Crossley, M;
- Details
- Publication Year 2004-09-17,Volume 279,Issue #38,Page 39789-39797
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Publication Type
- Journal Article
- 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.
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Keywords
- AMBIGUOUS DISTANCE RESTRAINTS; TRANSCRIPTIONAL COFACTOR FOG; PROTEIN-PROTEIN INTERACTIONS; CRYSTAL-STRUCTURE; NMR; FAMILY; PROGRAM; GENE; COMPLEX; TACC3
- Publisher's Version
- https://doi.org/10.1074/jbc.M404130200
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-09-17 12:00:00