Restructured transactivation domain in hamster AH receptor

Korkalainen, M; Tuomisto, J; Pohjanvirta, R

HERO ID

199003

Reference Type

Journal Article

Year

2000

Language

English

PMID

10873598

HERO ID 199003
In Press No
Year 2000
Title Restructured transactivation domain in hamster AH receptor
Authors Korkalainen, M; Tuomisto, J; Pohjanvirta, R
Journal Biochemical and Biophysical Research Communications
Volume 273
Issue 1
Page Numbers 272-281
Abstract 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.
Doi 10.1006/bbrc.2000.2931
Pmid 10873598
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English
Keyword 2,3,7,8-tetrachlorodibenzo-p-dioxin; TCDD; Aryl hydrocarbon receptor; Hamster; Cloning; Transactivation; Species differences
Is Qa No