The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein
Pitkanen, J ; Doucas, V ; Sternsdorf, T ; Nakajima, T ; Aratani, S ; Jensen, K ; Will, H ; Vahamurto, P ; Ollila, J and Vihinen, Mauno LU
, et al.
(2000)
In Journal of Biological Chemistry
275(22).
p.16802-16809
- Abstract
- Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy, caused by mutations in the autoimmune regulator (AIRE) gene, is an autosomal recessive autoimmune disease characterized by the breakdown of tolerance to organ-specific antigens. The 545 amino acid protein encoded by AIRE contains several structural motifs suggestive of a transcriptional regulator and bears similarity to cellular proteins involved in transcriptional control. me show here that AIRE fused to a heterologous DNA binding domain activates transcription from a reporter promoter, and the activation seen requires the full-length protein or more than one activation domain. At the structural level AIRE forms homodimers through the NH2-terminal domain, and molecular... (More)
- Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy, caused by mutations in the autoimmune regulator (AIRE) gene, is an autosomal recessive autoimmune disease characterized by the breakdown of tolerance to organ-specific antigens. The 545 amino acid protein encoded by AIRE contains several structural motifs suggestive of a transcriptional regulator and bears similarity to cellular proteins involved in transcriptional control. me show here that AIRE fused to a heterologous DNA binding domain activates transcription from a reporter promoter, and the activation seen requires the full-length protein or more than one activation domain. At the structural level AIRE forms homodimers through the NH2-terminal domain, and molecular modeling for this domain suggests a four-helix bundle structure. In agreement, we show that the common transcriptional coactivator CREB-binding protein (CBP) interacts with AIRE in vitro and in yeast nuclei through the CH1 and CH3 conserved domains. We suggest that the transcriptional transactivation properties of AIRE together with its interaction with CBP might be important in its function as disease-causing mutations almost totally abolish the activation effect. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3852045
- author
- Pitkanen, J
; Doucas, V
; Sternsdorf, T
; Nakajima, T
; Aratani, S
; Jensen, K
; Will, H
; Vahamurto, P
; Ollila, J
and Vihinen, Mauno
LU
, et al. (More)
- Pitkanen, J
; Doucas, V
; Sternsdorf, T
; Nakajima, T
; Aratani, S
; Jensen, K
; Will, H
; Vahamurto, P
; Ollila, J
; Vihinen, Mauno
LU
; Scott, HS
; Antonarakis, SE
; Kudoh, J
; Shimizu, N
; Krohn, K
and Peterson, P
(Less)
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 275
- issue
- 22
- pages
- 16802 - 16809
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000087392200058
- scopus:0038824426
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M908944199
- language
- English
- LU publication?
- no
- id
- 91d6e244-8ff4-4b05-8108-d0750f90275b (old id 3852045)
- date added to LUP
- 2016-04-01 12:00:06
- date last changed
- 2022-02-11 00:36:52
@article{91d6e244-8ff4-4b05-8108-d0750f90275b,
abstract = {{Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy, caused by mutations in the autoimmune regulator (AIRE) gene, is an autosomal recessive autoimmune disease characterized by the breakdown of tolerance to organ-specific antigens. The 545 amino acid protein encoded by AIRE contains several structural motifs suggestive of a transcriptional regulator and bears similarity to cellular proteins involved in transcriptional control. me show here that AIRE fused to a heterologous DNA binding domain activates transcription from a reporter promoter, and the activation seen requires the full-length protein or more than one activation domain. At the structural level AIRE forms homodimers through the NH2-terminal domain, and molecular modeling for this domain suggests a four-helix bundle structure. In agreement, we show that the common transcriptional coactivator CREB-binding protein (CBP) interacts with AIRE in vitro and in yeast nuclei through the CH1 and CH3 conserved domains. We suggest that the transcriptional transactivation properties of AIRE together with its interaction with CBP might be important in its function as disease-causing mutations almost totally abolish the activation effect.}},
author = {{Pitkanen, J and Doucas, V and Sternsdorf, T and Nakajima, T and Aratani, S and Jensen, K and Will, H and Vahamurto, P and Ollila, J and Vihinen, Mauno and Scott, HS and Antonarakis, SE and Kudoh, J and Shimizu, N and Krohn, K and Peterson, P}},
issn = {{1083-351X}},
language = {{eng}},
number = {{22}},
pages = {{16802--16809}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein}},
url = {{http://dx.doi.org/10.1074/jbc.M908944199}},
doi = {{10.1074/jbc.M908944199}},
volume = {{275}},
year = {{2000}},
}