| First Author | Korkalainen M | Year | 2000 |
| Journal | Biochem Biophys Res Commun | Volume | 273 |
| Issue | 1 | Pages | 272-81 |
| PubMed ID | 10873598 | Mgi Jnum | J:62892 |
| Mgi Id | MGI:1860021 | Doi | 10.1006/bbrc.2000.2931 |
| Citation | Korkalainen M, et al. (2000) Restructured transactivation domain in hamster AH receptor. Biochem Biophys Res Commun 273(1):272-81 |
| abstractText | Hamsters and Han/Wistar (Kuopio; H/W) rats show peculiarly selective responsiveness 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). Recent studies on H/W rat AHR discovered a remodelled transactivation domain which appears to be critical for the TCDD resistance of these animals. Here, molecular cloning and sequencing of hamster AHR reveals another type of restructured transactivation domain. In hamsters, the functionally pivotal Q-rich region is substantially expanded and enriched in glutamine compared with all other AHRs cloned to date. By contrast, the amino-terminal end is highly conserved, which is in agreement with the H/W rat AHR. Because of the additional material in the transactivation domain, hamster AHR protein is larger than that in rats or mice, but the pattern of AHR mRNA expression in tissues is similar. Copyright 2000 Academic Press. |
