Fluorescent Chemosensors for Divalent Zinc Based on Zinc Finger Domains. Enhanced Oxidative Stability, Metal Binding Affinity, and Structural and Functional Characterization

1997 ◽  
Vol 119 (15) ◽  
pp. 3443-3450 ◽  
Author(s):  
Grant K. Walkup ◽  
Barbara Imperiali
Keyword(s):  
Oxidative Stability ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Metal Binding ◽  
Functional Characterization ◽  
Fluorescent Chemosensors ◽  
Zinc Finger Domains

Insilico Search for Potential DNA Binding Domain of Human Zinc Finger Protein Sp1

2021 ◽  
pp. 217-225
Author(s):  
Sirisha Kaniganti
Keyword(s):  
Dna Binding ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Housekeeping Genes ◽  
Specificity Protein 1 ◽  
Finger Protein ◽  
Zinc Finger Domains ◽  
Specificity Protein ◽  
Regulation Of Growth

Specificity protein 1 (Sp1) belongs to a family of ubiquitously expressed, C2H2-type zinc finger-containing DNA binding proteins that activate or repress transcription of many genes in response to physiological and pathological stimuli. Specificity protein 1 is considered to be a constitutively expressed transcription factor and has been implicated in the regulation of a wide variety of housekeeping genes, tissue-specific genes, and genes involved in the regulation of growth. In order to determine the binding affinity of Sp1 zinc finger domains, the total energy for each and every possible combination of GC box and Zn finger motifs using Hex server, Model IT software’s is calculated. According to the findings of this study, the design of multi-zinc finger proteins with a variety of sequence specificities will be easier to accomplish. Among the three motifs present in Specificity protein 1, motifs 1 and 2 have higher binding affinity than motif 3.

scholarly journals Purification and properties of rat cysteine-rich intestinal protein

1994 ◽  
Vol 299 (2) ◽  
pp. 445-450 ◽  
Author(s):  
C Khoo ◽  
R J Cousins
Keyword(s):  
Small Intestine ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Metal Binding ◽  
Tissue Concentration ◽  
Exchange Chromatography ◽  
Zinc Binding ◽  
Intestinal Lumen ◽  
Intestinal Protein

Cysteine-rich intestinal protein (CRIP) is a zinc-binding protein where the binding domain is in the so-called LIM double zinc finger motif. Methods are described for the preparation of CRIP from rat small intestine. Gel-filtration and ion-exchange chromatography and preparative PAGE gave homogeneous CRIP, based upon analytical PAGE, mass spectrometry and microsequencing. Initial localization of CRIP during chromatography was based on binding of 65Zn radioisotope introduced into the intestine. The stoichiometry of binding by CRIP is less than 2 atoms of zinc per molecule. The metal-binding affinity in vitro is zinc > cadmium > copper > iron, at low metal concentrations. Zinc is the predominant metal bound when these metals are taken up from the intestinal lumen. Zinc binding was not influenced by pH between values of 4.5 to 7.5. Metallothionein has a much greater zinc-binding affinity than CRIP. The tissue concentration of CRIP is of the order of 15-20 micrograms/g of mucosal tissue, suggesting that the protein is more abundant than zinc-finger-containing transcription factors. The metal-binding properties of CRIP are consistent with proposed zinc-related functions for this cytoplasmic protein, which is expressed in the small intestine during the postnatal period.

A consensus zinc finger peptide: design, high-affinity metal binding, a pH-dependent structure, and a His to Cys sequence variant

1991 ◽  
Vol 113 (12) ◽  
pp. 4518-4523 ◽  
Author(s):  
Beth Allyn Krizek ◽  
Barbara T. Amann ◽  
Valda J. Kilfoil ◽  
Denise L. Merkle ◽  
Jeremy M. Berg
Keyword(s):  
Zinc Finger ◽  
Metal Binding ◽  
Sequence Variant ◽  
Peptide Design ◽  
High Affinity ◽  
Ph Dependent ◽  
Zinc Finger Peptide

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 Functional characterization of Lilium lancifolium cold-responsive Zinc Finger Homeodomain (ZFHD) gene in abscisic acid and osmotic stress tolerance

PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e11508
Author(s):  
Yubing Yong ◽  
Yue Zhang ◽  
Yingmin Lyu
Keyword(s):  
Abscisic Acid ◽  
Transgenic Plants ◽  
Zinc Finger ◽  
Promoter Region ◽  
Salt Water ◽  
Functional Characterization ◽  
Regulatory Elements ◽  
Response Analysis ◽  
Lilium Lancifolium

Background. We have previously performed an analysis of the cold-responsive transcriptome in the mature leaves of tiger lily (Lilium lancifolium) by gene co-expression network identification. The results has revealed that a ZFHD gene, notated as encoding zinc finger homeodomain protein, may play an essential regulating role in tiger lily response to cold stress. Methods. A further investigation of the ZFHD gene (termed as LlZFHD4) responding to osmotic stresses, including cold, salt, water stresses, and abscisic acid (ABA) was performed in this study. Based on the transcriptome sequences, the coding region and 5′ promoter region of LlZFHD4 were cloned from mature tiger lily leaves. Stress response analysis was performed under continuous 4 °C, NaCl, PEG, and ABA treatments. Functional characterization of LlZFHD4 was conducted in transgenic Arabidopsis, tobacco, and yeast. Results. LlZFHD4 encodes a nuclear-localized protein consisting of 180 amino acids. The N-terminal region of LlZFHD4 has transcriptional activation activity in yeast. The 4 °C, NaCl, PEG, and ABA treatments induced the expression of LlZFHD4. Several stress- or hormone-responsive cis-acting regulatory elements (T-Box, BoxI. and ARF) and binding sites of transcription factors (MYC, DRE and W-box) were found in the core promoter region (789 bp) of LlZFHD4. Also, the GUS gene driven by LlZFHD4 promoter was up-regulated by cold, NaCl, water stresses, and ABA in Arabidopsis. Overexpression of LlZFHD4 improved cold and drought tolerance in transgenic Arabidopsis; higher survival rate and better osmotic adjustment capacity were observed in LlZFHD4 transgenic plants compared to wild type (WT) plants under 4 °C and PEG conditions. However, LlZFHD4 transgenic plants were less tolerant to salinity and more hypersensitive to ABA compared to WT plants. The transcript levels of stress- and ABA-responsive genes were much more up-regulated in LlZFHD4 transgenic Arabidopsis than WT. These results indicate LlZFHD4 is involved in ABA signaling pathway and plays a crucial role in regulating the response of tiger lily to cold, salt and water stresses.

scholarly journals Biochemical Activities of Highly Purified, Catalytically Active Human APOBEC3G: Correlation with Antiviral Effect

2006 ◽  
Vol 80 (12) ◽  
pp. 5992-6002 ◽  
Author(s):  
Yasumasa Iwatani ◽  
Hiroaki Takeuchi ◽  
Klaus Strebel ◽  
Judith G. Levin
Keyword(s):  
Zinc Finger ◽  
Cytidine Deaminase ◽  
Antiviral Effect ◽  
Minimum Length ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Pure System ◽  
Dna And Rna ◽  
Catalytically Active ◽  
Zinc Finger Domains

ABSTRACT APOBEC3G (APO3G), a cytidine deaminase with two zinc finger domains, inhibits human immunodeficiency virus type 1 replication in the absence of Vif. Here, we provide a comprehensive molecular analysis of the deaminase and nucleic acid binding activities of human APO3G using a pure system containing only one protein component, i.e., highly purified, catalytically active enzyme expressed in a baculovirus system. We demonstrate that APO3G deaminates cytosines in single-stranded DNA (ssDNA) only, whereas it binds efficiently to ssDNA and ssRNA, about half as well to a DNA/RNA hybrid, and poorly to double-stranded DNA and RNA. In addition, the base specificities for deamination and binding of ssDNA are not correlated. The minimum length required for detection of APO3G binding to an ssDNA oligonucleotide in an electrophoretic mobility shift assay is 16 nucleotides. Interestingly, if nucleocapsid protein and APO3G are present in the same reaction, we find that they do not interfere with each other's binding to RNA and a complex containing the RNA and both proteins is formed. Finally, we also identify the functional activities of each zinc finger domain. Thus, although both zinc finger domains have the ability to bind nucleic acids, the first zinc finger contributes more to binding and APO3G encapsidation into virions than finger two. In contrast, deamination is associated exclusively with the second zinc finger. Moreover, zinc finger two is more important than finger one for the antiviral effect, demonstrating a correlation between deaminase and antiviral activities.

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