scholarly journals Sequence-specific DNA binding activity of the cross-brace zinc finger motif of the piggyBac transposase

2018 ◽  
Vol 46 (5) ◽  
pp. 2660-2677 ◽  
Author(s):  
Nelly Morellet ◽  
Xianghong Li ◽  
Silke A Wieninger ◽  
Jennifer L Taylor ◽  
Julien Bischerour ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Activity ◽  
Zinc Finger Motif ◽  
Dna Binding Activity ◽  
The Cross

scholarly journals The Human Monocytic Leukemia Zinc Finger Histone Acetyltransferase Domain Contains DNA-binding Activity Implicated in Chromatin Targeting

2007 ◽  
Vol 282 (50) ◽  
pp. 36603-36613 ◽  
Author(s):  
Marc A. Holbert ◽  
Timothy Sikorski ◽  
Juliana Carten ◽  
Danielle Snowflack ◽  
Santosh Hodawadekar ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Histone Acetyltransferase ◽  
Binding Activity ◽  
Monocytic Leukemia ◽  
Dna Binding Activity ◽  
Human Monocytic Leukemia ◽  
Acetyltransferase Domain

Characterization of the DNA Binding Activity of the ZFY Zinc Finger Domain

Biochemistry ◽  
2010 ◽  
Vol 49 (4) ◽  
pp. 679-686 ◽  
Author(s):  
Jennifer Grants ◽  
Erin Flanagan ◽  
Andrea Yee ◽  
Paul J. Romaniuk
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Activity ◽  
Zinc Finger Domain ◽  
Dna Binding Activity

scholarly journals Identification, nuclear localization, and DNA-binding activity of the zinc finger protein encoded by the Evi-1 myeloid transforming gene.

1990 ◽  
Vol 10 (3) ◽  
pp. 1259-1264 ◽  
Author(s):  
T Matsugi ◽  
K Morishita ◽  
J N Ihle
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Protein ◽  
Zinc Finger Protein ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Double Stranded Dna ◽  
Finger Protein ◽  
Myeloid Leukemias ◽  
Transforming Gene

Activation of the Evi-1 zinc finger gene is a common event associated with transformation of murine myeloid leukemias. To characterize the gene product, we developed antisera against various protein domains. These antisera primarily detected a 145-kilodalton nuclear protein that bound double-stranded DNA. Binding was inhibited by chelating agents and partially restored by zinc ions.

Identification, nuclear localization, and DNA-binding activity of the zinc finger protein encoded by the Evi-1 myeloid transforming gene

1990 ◽  
Vol 10 (3) ◽  
pp. 1259-1264
Author(s):  
T Matsugi ◽  
K Morishita ◽  
J N Ihle
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Protein ◽  
Zinc Finger Protein ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Double Stranded Dna ◽  
Finger Protein ◽  
Myeloid Leukemias ◽  
Transforming Gene

Activation of the Evi-1 zinc finger gene is a common event associated with transformation of murine myeloid leukemias. To characterize the gene product, we developed antisera against various protein domains. These antisera primarily detected a 145-kilodalton nuclear protein that bound double-stranded DNA. Binding was inhibited by chelating agents and partially restored by zinc ions.

Cysteine residues in the zinc finger and amino acids adjacent to the finger are necessary for DNA binding by the LAC9 regulatory protein of Kluyveromyces lactis

1988 ◽  
Vol 8 (9) ◽  
pp. 3726-3733
Author(s):  
M M Witte ◽  
R C Dickson
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Zinc Finger ◽  
Kluyveromyces Lactis ◽  
Regulatory Protein ◽  
Binding Activity ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Dna Binding Activity ◽  
Carboxyl Terminal

LAC9 is a positive regulatory protein that controls transcription of the lactose-galactose regulon in Kluyveromyces lactis. LAC9 is homologous to the GAL4 protein of Saccharomyces cerevisiae. Both proteins have a single "zinc finger" which plays a role in DNA binding. We previously hypothesized (L. V. Wray, M. M. Witte, R. C. Dickson, and M. I. Riley, Mol. Cell. Biol. 7:1111-1121, 1987) that the DNA-binding domain of the LAC9 protein consisted of the zinc finger as well as a region of amino acids on the carboxyl-terminal side of the zinc finger. In this study we used oligonucleotide-directed mutagenesis to introduce 13 single-amino-acid changes into the proposed DNA-binding domain of the LAC9 protein. Variant LAC9 proteins carrying an amino acid substitution in any one of the four highly conserved Cys residues of the zinc finger had reduced DNA-binding activity, suggesting that each Cys is necessary for DNA binding. Three of four variant LAC9 proteins with amino acid substitutions located on the carboxyl-terminal side of the zinc finger had reduced DNA-binding activity. These results support our hypothesis that the DNA-binding domain of the LAC9 protein is composed of the zinc finger and the adjacent region on the carboxyl side of the zinc finger, a region that has the potential to form an alpha-helix. Finally, LAC9 proteins containing His residues substituted for the conserved Cys residues also had reduced DNA-binding activity, indicating that His residues are not equivalent to Cys residues, as had been previously thought.

scholarly journals GATA-4 and Nkx-2.5 Coactivate Nkx-2 DNA Binding Targets: Role for Regulating Early Cardiac Gene Expression

1998 ◽  
Vol 18 (6) ◽  
pp. 3405-3415 ◽  
Author(s):  
Jorge L. Sepulveda ◽  
Narashimaswamy Belaguli ◽  
Vishal Nigam ◽  
Ching-Yi Chen ◽  
Mona Nemer ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Transcriptional Activation ◽  
Transcriptional Activity ◽  
Cardiac Tissue ◽  
Serum Response Factor ◽  
Binding Activity ◽  
Activation Domain ◽  
Dna Binding Activity ◽  
Inhibitory Domain

ABSTRACT The cardiogenic homeodomain factor Nkx-2.5 and serum response factor (SRF) provide strong transcriptional coactivation of the cardiac α-actin (αCA) promoter in fibroblasts (C. Y. Chen and R. J. Schwartz, Mol. Cell. Biol. 16:6372–6384, 1996). We demonstrate here that Nkx-2.5 also cooperates with GATA-4, a dual C-4 zinc finger transcription factor expressed in early cardiac progenitor cells, to activate the αCA promoter and a minimal promoter, containing only multimerized Nkx-2.5 DNA binding sites (NKEs), in heterologous CV-1 fibroblasts. Transcriptional activity requires the N-terminal activation domain of Nkx-2.5 and Nkx-2.5 binding activity through its homeodomain but does not require GATA-4’s activation domain. The minimal interactive regions were mapped to the homeodomain of Nkx-2.5 and the second zinc finger of GATA-4. Removal of Nkx-2.5’s C-terminal inhibitory domain stimulated robust transcriptional activity, comparable to the effects of GATA-4 on wild-type Nkx-2.5, which in part facilitated Nkx-2.5 DNA binding activity. We postulate the following simple model: GATA-4 induces a conformational change in Nkx-2.5 that displaces the C-terminal inhibitory domain, thus eliciting transcriptional activation of promoters containing Nkx-2.5 DNA binding targets. Therefore, αCa promoter activity appears to be regulated through the combinatorial interactions of at least three cardiac tissue-enriched transcription factors, Nkx-2.5, GATA-4, and SRF.

scholarly journals Dual histone methyl reader ZCWPW1 facilitates repair of meiotic double strand breaks in male mice

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Mohamed Mahgoub ◽  
Jacob Paiano ◽  
Melania Bruno ◽  
Wei Wu ◽  
Sarath Pathuri ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Histone Methylation ◽  
Genetic Recombination ◽  
Binding Activity ◽  
Double Strand Breaks ◽  
Gene Promoters ◽  
Male Mice ◽  
Strand Breaks ◽  
Dna Binding Activity

Meiotic crossovers result from homology-directed repair of DNA double-strand breaks (DSBs). Unlike yeast and plants, where DSBs are generated near gene promoters, in many vertebrates DSBs are enriched at hotspots determined by the DNA binding activity of the rapidly evolving zinc finger array of PRDM9 (PR domain zinc finger protein 9). PRDM9 subsequently catalyzes tri-methylation of lysine 4 and lysine 36 of Histone H3 in nearby nucleosomes. Here, we identify the dual histone methylation reader ZCWPW1, which is tightly co-expressed during spermatogenesis with Prdm9, as an essential meiotic recombination factor required for efficient repair of PRDM9-dependent DSBs and for pairing of homologous chromosomes in male mice. In sum, our results indicate that the evolution of a dual histone methylation writer/reader (PRDM9/ZCWPW1) system in vertebrates remodeled genetic recombination hotspot selection from an ancestral static pattern near genes towards a flexible pattern controlled by the rapidly evolving DNA binding activity of PRDM9.

Sign in / Sign up

Export Citation Format

Share Document