Transcriptional regulation of human eosinophil RNases by an evolutionary- conserved sequence motif in primate genome View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-12

AUTHORS

Hsiu-Yu Wang, Hao-Teng Chang, Tun-Wen Pai, Chung-I Wu, Yuan-Hung Lee, Yen-Hsin Chang, Hsiu-Ling Tai, Chuan-Yi Tang, Wei-Yao Chou, Margaret Dah-Tsyr Chang

ABSTRACT

BACKGROUND: Human eosinophil-derived neurotoxin (edn) and eosinophil cationic protein (ecp) are members of a subfamily of primate ribonuclease (rnase) genes. Although they are generated by gene duplication event, distinct edn and ecp expression profile in various tissues have been reported. RESULTS: In this study, we obtained the upstream promoter sequences of several representative primate eosinophil rnases. Bioinformatic analysis revealed the presence of a shared 34-nucleotide (nt) sequence stretch located at -81 to -48 in all edn promoters and macaque ecp promoter. Such a unique sequence motif constituted a region essential for transactivation of human edn in hepatocellular carcinoma cells. Gel electrophoretic mobility shift assay, transient transfection and scanning mutagenesis experiments allowed us to identify binding sites for two transcription factors, Myc-associated zinc finger protein (MAZ) and SV-40 protein-1 (Sp1), within the 34-nt segment. Subsequent in vitro and in vivo binding assays demonstrated a direct molecular interaction between this 34-nt region and MAZ and Sp1. Interestingly, overexpression of MAZ and Sp1 respectively repressed and enhanced edn promoter activity. The regulatory transactivation motif was mapped to the evolutionarily conserved -74/-65 region of the edn promoter, which was guanidine-rich and critical for recognition by both transcription factors. CONCLUSION: Our results provide the first direct evidence that MAZ and Sp1 play important roles on the transcriptional activation of the human edn promoter through specific binding to a 34-nt segment present in representative primate eosinophil rnase promoters. More... »

PAGES

89

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1471-2199-8-89

DOI

http://dx.doi.org/10.1186/1471-2199-8-89

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030876823

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17927842


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