caa a22 4500 397494041 CHVBK 20180308164516.0 cr unu---uuuuu 161202e199503 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124736 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124736 Structure and Regulation of the Chicken GATA-3 Gene [Elektronische Daten] [Hajime Ishihara, James Douglas Engel, Masayuki Yamamoto] To elucidate the mechanisms underlying the tissue-restricted expression of GATA factor transcription, we have isolated and analyzed the genomic chicken GATA-3 (cGATA-3) locus. Structural analysis of the clones showed that the cGATA-3 gene consists of six exons which span more than 19 kb. Two trans-activating domains and two Zn finger domains of cGATA-3 were found to be encoded separately by exons 2/3 and 4/5, respectively, indicating that each functional domain of GATA-3 is encoded by a discrete exon. We have determined 1.7 kb of upstream promoter sequence and found a number of sequence motifs which match those of known transcription factor binding sites. Activities of presumptive regulatory regions of this gene were assessed by transfecting chimeric constructs into a chicken T cell line MSB-1. The results showed three features of cGATA-3 gene regulation. The basal promoter activity of the cGATA-3 gene is determined by sequences lying between -104 and - 29 bp of the promoter region. The upstream region containing the GATA and CACCC elements in close proximity ( - 1280 to -1152) appeared to act as a negative transcriptional regulator, whereas the region -1151 to -850 acts as a positive regulator. Thus, the expression of cGATA-3 gene is under complex regulation and the mode of regulation of cGATA-3 gene expression is suggested to be different from that of GATA-1 genes. © 1995 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence GATA-3 nationallicence T cell nationallicence transcription factor nationallicence transcriptional regulation nationallicence Ishihara Hajime Department of Biochemistry, Tohoku University School of Medicine 2-1 Seiryomachi, Aoba-ku, Sendai 980-77 aut Engel James Douglas Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University Evanston, IL 60208-3500, USA aut Yamamoto Masayuki Department of Biochemistry, Tohoku University School of Medicine 2-1 Seiryomachi, Aoba-ku, Sendai 980-77 aut The Journal of Biochemistry Oxford University Press 117/3(1995-03), 499-508 0021-924X 117:3<499 1995 117 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124736 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124736 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ishihara Hajime Department of Biochemistry, Tohoku University School of Medicine 2-1 Seiryomachi, Aoba-ku, Sendai 980-77 aut NATIONALLICENCE 700 1- Engel James Douglas Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University Evanston, IL 60208-3500, USA aut NATIONALLICENCE 700 1- Yamamoto Masayuki Department of Biochemistry, Tohoku University School of Medicine 2-1 Seiryomachi, Aoba-ku, Sendai 980-77 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 117/3(1995-03), 499-508 0021-924X 117:3<499 1995 117 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford