Restructured transactivation domain in hamster AH receptor

Citation
M. Korkalainen et al., Restructured transactivation domain in hamster AH receptor, BIOC BIOP R, 273(1), 2000, pp. 272-281
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
273
Issue
1
Year of publication
2000
Pages
272 - 281
Database
ISI
SICI code
0006-291X(20000624)273:1<272:RTDIHA>2.0.ZU;2-0
Abstract
Hamsters and Han/Wistar (Kuopio; H/W) rats show peculiarly selective respon siveness to 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). They are extremely resistant to its acute lethality but sensitive to, e.g., enzyme induction. The biological effects of TCDD are mediated by the AH receptor (AHR). Recen t studies on H/W rat AHR discovered a remodelled transactivation domain whi ch appears to be critical for the TCDD resistance of these animals. Here, m olecular cloning and sequencing of hamster AHR reveals another type of rest ructured transactivation domain. In hamsters, the functionally pivotal Q-ri ch region is substantially expanded and enriched in glutamine compared with all other AHRs cloned to date. By contrast, the aminoterminal end is highl y conserved, which is in agreement with the H/W rat AHR. Because of the add itional material in the transactivation domain, hamster AHR protein is larg er than that in rats or mice, but the pattern of AHR mRNA expression in tis sues is similar. (C) 2000 Academic Press.