scholarly journals SpZ12-1, a negative regulator required for spatial control of the territory-specific CyIIIa gene in the sea urchin embryo

Development ◽  
1995 ◽  
Vol 121 (4) ◽  
pp. 1111-1122 ◽  
Author(s):  
D.G. Wang ◽  
C.V. Kirchhamer ◽  
R.J. Britten ◽  
E.H. Davidson
Keyword(s):  
Dna Binding ◽  
Sea Urchin ◽  
Fusion Gene ◽  
Binding Protein ◽  
Regulatory Element ◽  
Regulatory Region ◽  
Dna Binding Protein ◽  
Nuclear Extract ◽  
Negative Regulator ◽  
Expression Library

The CyIIIa cytoskeletal actin gene of the sea urchin Strongylocentrotus purpuratus is activated in late cleavage and expressed exclusively in the aboral ectoderm territory of the embryo. Previous gene transfer studies defined a 2.3 kb cis-regulatory region that is necessary and sufficient for correct temporal and spatial expression of a CyIIIa.CAT fusion gene. In this paper, a negative regulatory element within this region was identified that is required for repression of the CyIIIa gene in skeletogenic mesenchyme cells. The repression mediated by this regulatory element takes place after initial territorial specification. A cDNA clone encoding a DNA-binding protein with twelve Zn fingers (SpZ12-1) was isolated by probing an expression library with this cis-element. Deletion analysis of the SpZ12-1 protein confirmed that a DNA-binding domain is located within the Zn finger region. SpZ12-1 is the only DNA-binding protein in embryo nuclear extract that interacts with the specific cis-target sites required for repression of CyIIIa.CAT in skeletogenic mesenchyme and is likely to be the trans factor that mediates this repression.

scholarly journals LIM Protein KyoT2 Negatively Regulates Transcription by Association with the RBP-J DNA-Binding Protein

1998 ◽  
Vol 18 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Yoshihito Taniguchi ◽  
Takahisa Furukawa ◽  
Tin Tun ◽  
Hua Han ◽  
Tasuku Honjo
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Negative Regulator ◽  
Nuclear Antigen ◽  
Differential Splicing ◽  
Barr Virus ◽  
Lim Domains ◽  
C Terminus

ABSTRACT The RBP-J/Su(H) DNA-binding protein plays a key role in transcriptional regulation by targeting Epstein-Barr virus nuclear antigen 2 (EBNA2) and the intracellular portions of Notch receptors to specific promoters. Using the yeast two-hybrid system, we isolated a LIM-only protein, KyoT, which physically interacts with RBP-J. Differential splicing gave rise to two transcripts of theKyoT gene, KyoT1 and KyoT2, that encoded proteins with four and two LIM domains, respectively. With differential splicing resulting in deletion of an exon, KyoT2 lacked two LIM domains from the C terminus and had a frameshift in the last exon, creating the RBP-J-binding region in the C terminus. KyoT1 had a negligible level of interaction with RBP-J. Strong expression of KyoT mRNAs was detected in skeletal muscle and lung, with a predominance of KyoT1 mRNA. When expressed in F9 embryonal carcinoma cells, KyoT1 and KyoT2 were localized in the cytoplasm and the nucleus, respectively. The binding site of KyoT2 on RBP-J overlaps those of EBNA2 and Notch1 but is distinct from that of Hairless, the negative regulator of RBP-J-mediated transcription in Drosophila. KyoT2 but not KyoT1 repressed the RBP-J-mediated transcriptional activation by EBNA2 and Notch1 by competing with them for binding to RBP-J and by dislocating RBP-J from DNA. KyoT2 is a novel negative regulatory molecule for RBP-J-mediated transcription in mammalian systems.

scholarly journals SpGCF1, a Sea Urchin Embryo DNA-Binding Protein, Exists as Five Nested Variants Encoded by a Single mRNA

1995 ◽  
Vol 169 (2) ◽  
pp. 713-727 ◽  
Author(s):  
Robert W. Zeller ◽  
James A. Coffman ◽  
Michael G. Harrington ◽  
Roy J. Britten ◽  
Eric H. Davidson
Keyword(s):  
Dna Binding ◽  
Sea Urchin ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Sea Urchin Embryo

scholarly journals Identification of a 30-Base Pair Regulatory Element and Novel DNA Binding Protein That Regulates the Human GLUT4 Promoter in Transgenic Mice

2000 ◽  
Vol 275 (31) ◽  
pp. 23666-23673 ◽  
Author(s):  
Katherine M. Oshel ◽  
John B. Knight ◽  
Kim T. Cao ◽  
Martin V. Thai ◽  
Ann Louise Olson
Keyword(s):  
Dna Binding ◽  
Transgenic Mice ◽  
Base Pair ◽  
Binding Protein ◽  
Regulatory Element ◽  
Dna Binding Protein

Diurnal regulation of a DNA binding protein to the period repeat sequence in the SCN nuclear extract of rat brain

1999 ◽  
Vol 65 (2) ◽  
pp. 211-215 ◽  
Author(s):  
Toshiyuki Hamada ◽  
Koichiro Kako ◽  
Hisanori Wakamatsu ◽  
Shigenobu Shibata ◽  
Shigenori Watanabe ◽  
...  
Keyword(s):  
Dna Binding ◽  
Rat Brain ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Nuclear Extract ◽  
Repeat Sequence ◽  
Diurnal Regulation

scholarly journals A lipopolysaccharide-induced DNA-binding protein for a class II gene in B cells is distinct from NF-kappa B

1989 ◽  
Vol 9 (8) ◽  
pp. 3184-3192
Author(s):  
E M Gravallese ◽  
M R Boothby ◽  
C M Smas ◽  
L H Glimcher
Keyword(s):  
B Cells ◽  
Dna Binding ◽  
Binding Site ◽  
Binding Protein ◽  
Regulatory Region ◽  
Dna Binding Protein ◽  
Class Ii ◽  
Nf Kappa B ◽  
Inducible Protein ◽  
Lps Treatment

Class II (Ia) major histocompatibility complex molecules are cell surface proteins normally expressed by a limited subset of cells of the immune system. These molecules regulate the activation of T cells and are required for the presentation of antigens and the initiation of immune responses. The expression of Ia in B cells is determined by both the developmental stage of the B cell and by certain external stimuli. It has been demonstrated previously that treatment of B cells with lipopolysaccharide (LPS) results in increased surface expression of Ia protein. However, we have confirmed that LPS treatment results in a significant decrease in mRNA encoding the Ia proteins which persists for at least 18 h. Within the upstream regulatory region of A alpha k, an NF-kappa B-like binding site is present. We have identified an LPS-induced DNA-binding protein in extracts from athymic mice whose spleens consist predominantly of B cells. Binding activity is present in low levels in unstimulated spleen cells and is increased by LPS treatment. This protein binds to two sites in a regulatory region of the Ia A alpha k gene, one of which contains the NF-kappa B-like binding site. DNA fragments containing these sites cross-compete for protein binding. Analysis by DNase I footprinting identified a target binding sequence, named the LPS-responsive element. Although this target sequence contains an NF-kappa B-like binding site, competition with a mutant oligonucleotide demonstrated that bases critical for NF-kappa B binding are not required for binding of the LPS-inducible protein. Therefore, we hypothesized that this inducible protein represents a new mediator of LPS action, distinct from NF-kappa B, and may be one mechanism to account for the decrease in mRNA encoding the Ia proteins.

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