scholarly journals Role of Zinc Finger Domains of the Transcription Factor Neuron-restrictive Silencer Factor/Repressor Element-1 Silencing Transcription Factor in DNA Binding and Nuclear Localization

2001 ◽  
Vol 276 (16) ◽  
pp. 13121-13126 ◽  
Author(s):  
Masahito Shimojo ◽  
Jeong-Heon Lee ◽  
Louis B. Hersh
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Zinc Finger Domains ◽  
Repressor Element

Bifunctional role of the zinc finger domains of the methyl-DNA-binding protein Kaiso

2010 ◽  
Vol 44 (2) ◽  
pp. 233-244 ◽  
Author(s):  
N. A. Zhigalova ◽  
S. V. Zhenilo ◽  
D. S. Aithozhina ◽  
E. B. Prokhortchouk
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Zinc Finger Domains

scholarly journals Identification of DNA Recognition Sequences and Protein Interaction Domains of the Multiple-Zn-Finger Protein Roaz

1998 ◽  
Vol 18 (11) ◽  
pp. 6447-6456 ◽  
Author(s):  
Robert Y. L. Tsai ◽  
Randall R. Reed
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Site ◽  
Zinc Finger ◽  
Protein Interaction ◽  
Inverted Repeat ◽  
Finger Protein ◽  
Zinc Finger Motifs ◽  
Half Site

ABSTRACT Roaz, a rat C2H2 zinc finger protein, plays a role in the regulation of olfactory neuronal differentiation through its interaction with the Olf-1/EBF transcription factor family. An additional role for the Roaz/Olf-1/EBF heterodimeric protein is suggested by its ability to regulate gene activation at a distinct promoter lacking Olf-1/EBF-binding sites. Using an in vitro binding-site selection assay (Selex), we demonstrate that Roaz protein binds to novel inverted perfect or imperfect repeats of GCACCC separated by 2 bp. We show that Roaz is capable of binding to a canonical consensus recognition sequence with high affinity (Kd = 3 nM). Analysis of the structural requirement for protein dimerization and DNA binding by Roaz reveals the role of specific zinc finger motifs in the Roaz protein for homodimerization and heterodimerization with the Olf-1/EBF transcription factor. The DNA-binding domain of Roaz is mapped to the N-terminal 277 amino acids, containing the first seven zinc finger motifs, which confers weak monomeric binding to a single half site and a stronger dimeric binding to the inverted repeat in a binding-site-dependent manner. Full-length protein can form dimers on both the inverted repeat and direct repeat but not on a single half site. These findings support the role of the TFIIIA-type Zn fingers in both protein-protein interaction and protein-DNA interaction and suggest distinct functions for specific motifs in proteins with a large number of zinc finger structures.

The role of the DNA-binding One Zinc Finger (DOF) transcription factor family in plants

Plant Science ◽  
2013 ◽  
Vol 209 ◽  
pp. 32-45 ◽  
Author(s):  
Mélanie Noguero ◽  
Rana Muhammad Atif ◽  
Sergio Ochatt ◽  
Richard D. Thompson
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Finger ◽  
Transcription Factor Family ◽  
Dof Transcription Factor

scholarly journals Ambient pH Signaling Regulates Nuclear Localization of the Aspergillus nidulans PacC Transcription Factor

2001 ◽  
Vol 21 (5) ◽  
pp. 1688-1699 ◽  
Author(s):  
José M. Mingot ◽  
Eduardo A. Espeso ◽  
Eliecer Dı́ez ◽  
MiguelÁ. Peñalva
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Aspergillus Nidulans ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Proteolytic Processing ◽  
Full Length ◽  
Alkaline Ph ◽  
Open Conformation ◽  
Processed Form

ABSTRACT The Aspergillus nidulans zinc finger transcription factor PacC is activated by proteolytic processing in response to ambient alkaline pH. The pH-regulated step is the transition of full-length PacC from a closed to an open, protease-accessible conformation. Here we show that in the absence of ambient pH signaling, the C-terminal negative-acting domain prevents the nuclear localization of full-length closed PacC. In contrast, the processed PacC form is almost exclusively nuclear at any ambient pH. In the presence of ambient pH signaling, the fraction of PacC that is in the open conformation but has not yet been processed localizes to the nucleus. Therefore, ambient alkaline pH leads to an increase in nuclear PacC by promoting the proteolytic elimination of the negative-acting domain to yield the processed form and by increasing the proportion of full-length protein that is in the open conformation. These findings explain why mutations resulting in commitment of PacC to processing irrespective of ambient pH lead to permanent PacC activation and alkalinity mimicry. A nuclear import signal that targetsEscherichia coli β-galactosidase to the nucleus has been located to the PacC zinc finger region. A mutation abolishing DNA binding does not prevent nuclear localization of the processed form, showing that PacC processing does not lead to nuclear localization by passive diffusion of the protein made possible by the reduction in size, followed by retention in the nucleus after DNA binding.

Role of zinc finger structure in nuclear localization of transcription factor Sp1

2009 ◽  
Vol 380 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Tatsuo Ito ◽  
Makiko Azumano ◽  
Chisana Uwatoko ◽  
Kohji Itoh ◽  
Jun Kuwahara
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Transcription Factor Sp1

scholarly journals Human GATA-3 trans-activation, DNA-binding, and nuclear localization activities are organized into distinct structural domains.

1994 ◽  
Vol 14 (3) ◽  
pp. 2201-2212 ◽  
Author(s):  
Z Yang ◽  
L Gu ◽  
P H Romeo ◽  
D Bories ◽  
H Motohashi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Structural Domains ◽  
Cellular Genes ◽  
Dna Binding Site ◽  
Discrete Domains ◽  
Definition Of ◽  
Site Recognition

GATA-3 is a zinc finger transcription factor which is expressed in a highly restricted and strongly conserved tissue distribution pattern in vertebrate organisms, specifically, in a subset of hematopoietic cells, in cells within the central and peripheral nervous systems, in the kidney, and in placental trophoblasts. Tissue-specific cellular genes regulated by GATA-3 have been identified in T lymphocytes and the placenta, while GATA-3-regulated genes in the nervous system and kidney have not yet been defined. We prepared monoclonal antibodies with which we could dissect the biochemical and functional properties of human GATA-3. The results of these experiments show some anticipated phenotypes, for example, the definition of discrete domains required for specific DNA-binding site recognition (amino acids 303 to 348) and trans activation (amino acids 30 to 74). The signaling sequence for nuclear localization of human GATA-3 is a property conferred by sequences within and surrounding the amino finger (amino acids 249 to 311) of the protein, thereby assigning a function to this domain and thus explaining the curious observation that this zinc finger is dispensable for DNA binding by the GATA family of transcription factors.

scholarly journals Determination of DNA binding specificities of mutated zinc finger domains

FEBS Letters ◽  
1991 ◽  
Vol 283 (1) ◽  
pp. 23-26 ◽  
Author(s):  
Hans-Jürgen Thiesen ◽  
Christian Bach
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Zinc Finger Domains

scholarly journals Aβ-Induced Repressor Element 1-Silencing Transcription Factor (REST) Gene Delivery Suppresses Activation of Microglia-Like BV-2 Cells

2020 ◽  
Vol 2020 ◽  
pp. 1-8 ◽  
Author(s):  
Tongya Yu ◽  
Hui Quan ◽  
Yuzhen Xu ◽  
Yunxiao Dou ◽  
Feihong Wang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cell Proliferation ◽  
Transcription Factor ◽  
Cell Activation ◽  
Type I ◽  
Hairpin Rna ◽  
Cell Dysfunction ◽  
Repressor Element

Compelling evidence from basic molecular biology has demonstrated the crucial role of microglia in the pathogenesis of Alzheimer’s disease (AD). Microglia were believed to play a dual role in both promoting and inhibiting Alzheimer’s disease progression. It is of great significance to regulate the function of microglia and make them develop in a favorable way. In the present study, we investigated the function of repressor element 1-silencing transcription factor (REST) in Aβ1-42-induced BV-2 cell dysfunction. We concluded that Aβ1-42 could promote type I activation of BV-2 cells and induce cell proliferation, migration, and proinflammation cytokine TNF-α, IL-1β, and IL-6 expression. Meanwhile, REST was upregulated, and nuclear translocalization took place due to Aβ1-42 stimulation. When REST was knocked down by a specific short hairpin RNA (sh-RNA), BV-2 cell proliferation, migration, and proinflammation cytokine expression and secretion induced by Aβ1-42 were increased, demonstrating that REST may act as a repressor of microglia-like BV-2 cell activation.

Sign in / Sign up

Export Citation Format

Share Document