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

• We demonstrate that the cDNA encodes the specific Eryf1 binding activity found in erythrocytes [3].
• Finally, the factor can reprogram a v-Myc-transformed macrophage cell line into myeloblasts, eosinophils, and erythroblasts, showing that the effects of GATA-1 are not limited to Myb-Ets-transformed myeloblasts [4].
• GATA-1 reprograms avian myelomonocytic cell lines into eosinophils, thromboblasts, and erythroblasts [4].
• These genes contain a specialized TATA box at -30 (GATA) through which the erythroid-restricted protein cGATA-1 and TFIID both function to regulate different steps in beta-globin expression [5].
• The erythroid-specific protein cGATA-1 regulates the chick beta-globin gene through GATA sequences present at the canonical TATA location in the promoter as well as the distal 3' enhancer [6].

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

• Diagonal mobility-shift assays demonstrated that multisubunit complexes were forming with the GATA-1 protein [13].
• A molecular dissection of the interaction between the transcription factor Gata-1 zinc finger and DNA [14].
• Downstream of the three GATA-1 motifs which constitute the core enhancer, a 4th homology box, containing two further DNA binding motifs, was found by sequence alignment between duck and chicken [22].

References