InterPro domain: IPR039355

This entry represents proteins with GATA-type zinc fingers (Znf). A number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins) specifically bind the DNA sequence (A/T)GATA(A/G) [ 1 ] in the regulatory regions of genes. They are consequently termed GATA-binding transcription factors. The interactions occur via highly-conserved Znf domains in which the zinc ion is coordinated by four cysteine residues [ 2 , 3 ]. NMR studies have shown the core of the Znf to comprise two irregular anti-parallel beta-sheets and an alpha-helix, followed by a long loop to the C-terminal end of the finger. The N-terminal part, which includes the helix, is similar in structure, but not sequence, to the N-terminal zinc module of the glucocorticoid receptor DNA-binding domain. The helix and the loop connecting the two beta-sheets interact with the major groove of the DNA, while the C-terminal tail wraps around into the minor groove. It is this tail that is the essential determinant of specific binding. Interactions between the Znf and DNA are mainly hydrophobic, explaining the preponderance of thymines in the binding site; a large number of interactions with the phosphate backbone have also been observed [ 4 ]. Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contains a single copy of the domain.

The GATA-type transcription factors SreA and Sre1 from fungi regulate iron- acquisition genes [ 4 , 5 ].

1. Activity and tissue-specific expression of the transcription factor NF-E1 multigene family. Genes Dev. 4, 1650-62
2. The erythroid-specific transcription factor Eryf1: a new finger protein. Cell 58, 877-85
3. NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science 261, 438-46
4. SreA-mediated iron regulation in Aspergillus fumigatus. Mol. Microbiol. 70, 27-43
5. Iron, oxidative stress, and virulence: roles of iron-sensitive transcription factor Sre1 and the redox sensor ChAp1 in the maize pathogen Cochliobolus heterostrophus. Mol. Plant Microbe Interact. 26, 1473-85