Study on mechanisms of the expression regulation of interferon-induced gene RIG-G.
- Author:
Dong LI
1
;
Shu XIAO
;
Xiao-rong PAN
;
Ye-jiang LOU
;
Pei-min JIA
;
Jian-hua TONG
Author Information
- Publication Type:Journal Article
- MeSH: Base Sequence; Cells, Cultured; Gene Expression Regulation; drug effects; physiology; Humans; Interferon Regulatory Factor-1; genetics; metabolism; Interferon Regulatory Factors; genetics; metabolism; Interferon-alpha; pharmacology; physiology; Interferons; physiology; Molecular Sequence Data; Promoter Regions, Genetic; drug effects; genetics; physiology; STAT1 Transcription Factor; metabolism
- From: Chinese Journal of Medical Genetics 2007;24(6):625-628
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the molecular mechanisms of the expression regulation of retinoic acidinduced gene G (RIG-G) by interferon alpha (IFNalpha).
METHODSRIG-G promoter region was analyzed by bioinformatics. The functional activities of RIG-G promoter with or without IFNalpha were detected by luciferase reporter assay and electrophoretic mobility shift assay (EMSA).
RESULTSRIG-G promoter region contained two well-conserved IFN-stimulated response elements (ISREs). Both ISRE I and ISRE II showed their effective binding abilities with signal transducer and activator of transcription 1 (STAT1). In HT1080 cells, in contrast with the empty plasmid pXP2, pXP2-A reporter construct containing intact ISRE I and ISRE II showed a significant higher baseline expression (1741.2 +/- 517.5) which could be further enhanced up to three-four folds by IFNalpha (5338.7 +/- 1226.9, P < 0.05). However, the luciferase activity of pXP2-A as well as its IFNalpha inducibility could be abrogated in STAT1-deficient U3A cells (from 1741.2 +/- 517.5 to 406.1 +/- 103.2, P < 0.05), indicating that the STAT1 protein was a prerequisite for the activities of ISRE I and ISRE II.
CONCLUSIONISREs present in RIG-G promoter region are molecular basis of IFNalpha induced RIG-G expression. RIG-G is a target gene directly regulated by STAT1 protein and should play a key role in IFNalpha signaling pathways.
