scholarly journals Analysis of the PAX interacting (with transcription-activation domain) protein 1 (Paxip1)-regulated transcriptome in mouse embryonic fibroblasts

2016 ◽  
Author(s):  
Y Cho
Keyword(s):  
Transcription Activation ◽  
Mouse Embryonic Fibroblasts ◽  
Activation Domain ◽  
Embryonic Fibroblasts ◽  
Transcription Activation Domain ◽  
Domain Protein

scholarly journals Direct photoresponsive inhibition of a p53-like transcription activation domain in PIF3 by Arabidopsis phytochrome B

2021 ◽  
Author(s):  
Chan Yul Yoo ◽  
Qing Sang ◽  
Jiangman He ◽  
Yongjian Qiu ◽  
Lingyun Long ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Target Genes ◽  
Transcription Activation ◽  
Phytochrome B ◽  
Activation Domain ◽  
Light Responses ◽  
Dark Light ◽  
Transactivation Activity ◽  
Transcription Activation Domain

Phytochrome B (PHYB) triggers diverse light responses in Arabidopsis by binding to a group of antagonistically acting PHYTOCHROME-INTERACTING transcription FACTORs (PIFs) to promote PIF degradation, consequently downregulating PIF target genes. However, whether PHYB directly controls the transactivation activity of PIFs remains ambiguous. Here we show that the prototypic PIF, PIF3, possesses a p53-like transcription activation domain (TAD) consisting of a sequence-specific, hydrophobic activator motif surrounded by acidic residues. A PIF3mTAD mutant in which the activator motif is replaced with alanines fails to activate PIF3 target genes in Arabidopsis in dark, light, and shade conditions, validating the in vivo functions of the PIF3 TAD. Intriguingly, binding of the N-terminal photosensory module of PHYB to the PHYB-binding site adjacent to the TAD inhibits its transactivation activity. These results unveil a photoresponsive transcriptional switching mechanism in which photoactivated PHYB directly masks the transactivation activity of PIF3. Our study also suggests the unexpected conservation of sequence-specific TADs between the animal and plant kingdoms.

Identification of Novel and Cell Type Enriched Cofactors of the Transcription Activation Domain of RelA (p65 NF-κB)

2005 ◽  
Vol 4 (4) ◽  
pp. 1381-1390 ◽  
Author(s):  
Heather R. Owen ◽  
Manfredo Quadroni ◽  
Willy Bienvenut ◽  
Christine Buerki ◽  
Michael O. Hottiger
Keyword(s):  
Transcription Activation ◽  
Cell Type ◽  
Activation Domain ◽  
Transcription Activation Domain

scholarly journals A tryptophan-rich peptide acts as a transcription activation domain

2010 ◽  
Vol 11 (1) ◽  
Author(s):  
Chen-Huan Lin ◽  
Grace Lin ◽  
Chia-Pei Chang ◽  
Chien-Chia Wang
Keyword(s):  
Transcription Activation ◽  
Activation Domain ◽  
Transcription Activation Domain

scholarly journals Multiple layers of regulation of human heat shock transcription factor 1.

1995 ◽  
Vol 15 (8) ◽  
pp. 4319-4330 ◽  
Author(s):  
J Zuo ◽  
D Rungger ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Dna Binding ◽  
Cell Activation ◽  
Transcription Activation ◽  
Heat Shock Transcription Factor ◽  
Activation Domain ◽  
Sequence Element ◽  
Transcription Activation Domain ◽  
Transcription Factor 1

Upon heat stress, monomeric human heat shock transcription factor 1 (hHSF1) is converted to a trimer, acquires DNA-binding ability, is transported to the nucleus, and becomes transcriptionally competent. It was not known previously whether these regulatory changes are caused by a single activation event or whether they occur independently from one another, providing a multilayered control that may prevent inadvertant activation of hHSF1. Comparison of wild-type and mutant hHSF1 expressed in Xenopus oocytes and human HeLa cells suggested that retention of hHSF1 in the monomeric form depends on hydrophobic repeats (LZ1 to LZ3) and a carboxy-terminal sequence element in hHSF1 as well as on the presence of a titratable factor in the cell. Oligomerization of hHSF1 appears to induce DNA-binding activity as well as to uncover an amino-terminally located nuclear localization signal. A mechanism distinct from that controlling oligomerization regulates the transcriptional competence of hHSF1. Components of this mechanism were mapped to a region, including LZ2 and nearby sequences downstream from LZ2, that is clearly separated from the carboxy-terminally located transcription activation domain(s). We propose the existence of a fold-back structure that masks the transcription activation domain in the unstressed cell but is opened up by modification of hHSF1 and/or binding of a factor facilitating hHSF1 unfolding in the stressed cell. Activation of hHSF1 appears to involve at least two independently regulated structural transitions.

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