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GATA1  -  GATA binding protein 1 (globin...

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Disease relevance of LOC396450

  • Each of these GATA-1 sites had an enhancer activity when inserted into a reporter plasmid and tested in human erythroleukemia cells [1].
  • GATA proteins are transcription factors that bind GATA DNA elements through Cys4 structural zinc-binding domains and play critical regulatory roles in neurological and urogenital development and the development of cardiac disease [2].

High impact information on LOC396450


Biological context of LOC396450

  • Hence, the differentiation-specific effect of the enhancers is not mediated by changes in relative levels of the GATA factors [7].
  • The method is demonstrated on a complex of the DNA-binding domain of the transcription factor GATA-1 with a 16 base pair oligodeoxyribonucleotide [8].
  • To understand the differences in the binding specificities of the N- and C-terminal zinc fingers of GATA-1, we have constructed a series of swapped domain peptides [9].
  • We show that, as in the case of some other members of the GATA gene family, the gene is expressed from alternative first exons [10].
  • Its binding site specificity is different from that of GATA-1, having a much higher affinity for the motif with a core GATC sequence [11].

Anatomical context of LOC396450

  • However, the role of GATA proteins in spinal cord development remains unresolved [12].
  • Members of the GATA transcription factor gene family have been implicated in a variety of developmental processes, including that of the vertebrate central nervous system [12].
  • GATA proteins identify a novel ventral interneuron subclass in the developing chick spinal cord [12].
  • In DNAase I footprinting and u.v. cross-linking experiments with nuclear extracts from adult chicken immature erythrocytes, we determined that the trans-acting factor GATA-1 was the predominating protein interacting with the histone H5 enhancer [13].
  • The prototypic member, GATA-1, is required for normal erythroid, megakaryocytic, and mast cell development [9].

Associations of LOC396450 with chemical compounds

  • The hypothesis that thymine methyl groups are important to the free energy of binding between Gata and DNA is tested by measuring binding of an oligonucleotide substrate in which individual thymine bases are substituted with uracil [14].
  • The cis-acting sequence in one of these regions (Region A) includes the core binding motif GATA, raising the possibility that this region of DNA mediates binding of a member of the GATA-binding protein family [15].
  • The structure of the C-terminal CCCC module is essentially identical to that observed for the DNA-interactive CCCC modules of the GATA-1 and steroid hormone receptor DNA binding domains, raising the possibility that the LIM motif may have a DNA binding function [16].
  • Phylogenetic analyses of HOX, GATA and EVX protein families demonstrate that polyalanine domains arose independently in different members of these families, suggesting that convergent molecular evolution may have played a role [17].
  • The chicken vitellogenin II gene is flanked by a GATA factor-dependent estrogen response unit [18].

Physical interactions of LOC396450

  • Gel-mobility-shift assays with 23 bp oligonucleotides containing the GATA-binding site (AGATAA) of the histone H5 enhancer or of the beta-globin enhancer showed that the GATA sequence was sufficient for the formation of at least five complexes [13].
  • A computer simulation analysis based on the solution structure of the chicken GATA1/DNA complex supported the importance of this motif in GATA3 DNA binding [19].

Other interactions of LOC396450

  • In this study, we investigated the expression and function of two GATA proteins, GATA2 and GATA3, in the developing chick spinal cord [12].
  • However, no coexpression is observed between the two GATA proteins and CHX10 [12].
  • Butyrate treatment of oocytes stimulated cap-site initiation by up to 17-fold with both normal promoter and GATA site mutant constructs, showing that the mechanism of butyrate stimulation is not via GATA-2 [11].
  • JB-transformed bone marrow cells expressed GATA-1, TAL-1, and histone H5, suggesting that they belong to the erythrocytic/thrombocytic lineage [20].
  • DNase I and micrococcal nuclease probes show that GATA-1 binding causes extensive, cooperative breakage of the histone/DNA contacts to generate a complex very similar to that formed by the factor with free DNA [21].

Analytical, diagnostic and therapeutic context of LOC396450


  1. Structure and function of the enhancer 3' to the human A gamma globin gene. Purucker, M., Bodine, D., Lin, H., McDonagh, K., Nienhuis, A.W. Nucleic Acids Res. (1990) [Pubmed]
  2. Spectroscopic and functional determination of the interaction of Pb2+ with GATA proteins. Ghering, A.B., Jenkins, L.M., Schenck, B.L., Deo, S., Mayer, R.A., Pikaart, M.J., Omichinski, J.G., Godwin, H.A. J. Am. Chem. Soc. (2005) [Pubmed]
  3. The erythroid-specific transcription factor Eryf1: a new finger protein. Evans, T., Felsenfeld, G. Cell (1989) [Pubmed]
  4. GATA-1 reprograms avian myelomonocytic cell lines into eosinophils, thromboblasts, and erythroblasts. Kulessa, H., Frampton, J., Graf, T. Genes Dev. (1995) [Pubmed]
  5. The erythroid protein cGATA-1 functions with a stage-specific factor to activate transcription of chromatin-assembled beta-globin genes. Barton, M.C., Madani, N., Emerson, B.M. Genes Dev. (1993) [Pubmed]
  6. The erythroid-specific protein cGATA-1 mediates distal enhancer activity through a specialized beta-globin TATA box. Fong, T.C., Emerson, B.M. Genes Dev. (1992) [Pubmed]
  7. Transcription of the histone H5 gene is regulated by three differentiation-specific enhancers. Rousseau, S., Asselin, M., Renaud, J., Ruiz-Carrillo, A. Mol. Cell. Biol. (1993) [Pubmed]
  8. Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Tjandra, N., Omichinski, J.G., Gronenborn, A.M., Clore, G.M., Bax, A. Nat. Struct. Biol. (1997) [Pubmed]
  9. Determinants of GATA-1 binding to DNA: the role of non-finger residues. Ghirlando, R., Trainor, C.D. J. Biol. Chem. (2003) [Pubmed]
  10. Alternate promoters and developmental modulation of expression of the chicken GATA-2 gene in hematopoietic progenitor cells. Nony, P., Hannon, R., Gould, H., Felsenfeld, G. J. Biol. Chem. (1998) [Pubmed]
  11. GATA-2 is a maternal transcription factor present in Xenopus oocytes as a nuclear complex which is maintained throughout early development. Partington, G.A., Bertwistle, D., Nicolas, R.H., Kee, W.J., Pizzey, J.A., Patient, R.K. Dev. Biol. (1997) [Pubmed]
  12. GATA proteins identify a novel ventral interneuron subclass in the developing chick spinal cord. Karunaratne, A., Hargrave, M., Poh, A., Yamada, T. Dev. Biol. (2002) [Pubmed]
  13. Multisubunit erythroid complexes binding to the enhancer element of the chicken histone H5 gene. Penner, C.G., Davie, J.R. Biochem. J. (1992) [Pubmed]
  14. A molecular dissection of the interaction between the transcription factor Gata-1 zinc finger and DNA. Mott, B.H., Bassman, J., Pikaart, M.J. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  15. Cloning of the GATA-binding protein that regulates endothelin-1 gene expression in endothelial cells. Lee, M.E., Temizer, D.H., Clifford, J.A., Quertermous, T. J. Biol. Chem. (1991) [Pubmed]
  16. Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP. Pérez-Alvarado, G.C., Miles, C., Michelsen, J.W., Louis, H.A., Winge, D.R., Beckerle, M.C., Summers, M.F. Nat. Struct. Biol. (1994) [Pubmed]
  17. Polymorphism, shared functions and convergent evolution of genes with sequences coding for polyalanine domains. Lavoie, H., Debeane, F., Trinh, Q.D., Turcotte, J.F., Corbeil-Girard, L.P., Dicaire, M.J., Saint-Denis, A., Pagé, M., Rouleau, G.A., Brais, B. Hum. Mol. Genet. (2003) [Pubmed]
  18. The chicken vitellogenin II gene is flanked by a GATA factor-dependent estrogen response unit. Davis, D.L., Burch, J.B. Mol. Endocrinol. (1996) [Pubmed]
  19. Critical YxKxHxxxRP Motif in the C-Terminal Region of GATA3 for Its DNA Binding and Function. Shinnakasu, R., Yamashita, M., Shinoda, K., Endo, Y., Hosokawa, H., Hasegawa, A., Ikemizu, S., Nakayama, T. J. Immunol. (2006) [Pubmed]
  20. v-jun cooperates with v-erbB to transform the thrombocytic/megakaryocytic lineage. Garcia, M., Samarut, J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  21. Perturbation of nucleosome structure by the erythroid transcription factor GATA-1. Boyes, J., Omichinski, J., Clark, D., Pikaart, M., Felsenfeld, G. J. Mol. Biol. (1998) [Pubmed]
  22. Analysis of the distribution of protein binding DNA motives in the vicinity of the 3'-side chicken alpha-globin enhancer. Targa, F.R., de Moura Gallo, C.V., Scherrer, K. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
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