Structural highlights
Function
[GATA1_MOUSE] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Zinc fingers (ZnFs) are generally regarded as DNA-binding motifs. However, a number of recent reports have implicated particular ZnFs in the mediation of protein-protein interactions. The N-terminal ZnF of GATA-1 (NF) is one such finger, having been shown to interact with a number of other proteins, including the recently discovered transcriptional co-factor FOG. Here we solve the three-dimensional structure of the NF in solution using multidimensional 1H/15N NMR spectroscopy, and we use 1H/15N spin relaxation measurements to investigate its backbone dynamics. The structure consists of two distorted beta-hairpins and a single alpha-helix, and is similar to that of the C-terminal ZnF of chicken GATA-1. Comparisons of the NF structure with those of other C4-type zinc binding motifs, including hormone receptor and LIM domains, also reveal substantial structural homology. Finally, we use the structure to map the spatial locations of NF residues shown by mutagenesis to be essential for FOG binding, and demonstrate that these residues all lie on a single face of the NF. Notably, this face is well removed from the putative DNA-binding face of the NF, an observation which is suggestive of simultaneous roles for the NF; that is, stabilisation of GATA-1 DNA complexes and recruitment of FOG to GATA-1-controlled promoter regions.
The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG.,Kowalski K, Czolij R, King GF, Crossley M, Mackay JP J Biomol NMR. 1999 Mar;13(3):249-62. PMID:10212985[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martin DI, Orkin SH. Transcriptional activation and DNA binding by the erythroid factor GF-1/NF-E1/Eryf 1. Genes Dev. 1990 Nov;4(11):1886-98. PMID:2276623
- ↑ Crossley M, Orkin SH. Phosphorylation of the erythroid transcription factor GATA-1. J Biol Chem. 1994 Jun 17;269(24):16589-96. PMID:8206977
- ↑ Calligaris R, Bottardi S, Cogoi S, Apezteguia I, Santoro C. Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11598-602. PMID:8524811
- ↑ Collavin L, Gostissa M, Avolio F, Secco P, Ronchi A, Santoro C, Del Sal G. Modification of the erythroid transcription factor GATA-1 by SUMO-1. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8870-5. Epub 2004 Jun 1. PMID:15173587 doi:http://dx.doi.org/10.1073/pnas.0308605101
- ↑ Lamonica JM, Vakoc CR, Blobel GA. Acetylation of GATA-1 is required for chromatin occupancy. Blood. 2006 Dec 1;108(12):3736-8. Epub 2006 Aug 3. PMID:16888089 doi:http://dx.doi.org/10.1182/blood-2006-07-032847
- ↑ Kowalski K, Czolij R, King GF, Crossley M, Mackay JP. The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG. J Biomol NMR. 1999 Mar;13(3):249-62. PMID:10212985
