scholarly journals Differential Binding of Monomethylarsonous Acid Compared to Arsenite and Arsenic Trioxide with Zinc Finger Peptides and Proteins

2014 ◽  
Vol 27 (4) ◽  
pp. 690-698 ◽  
Author(s):  
Xixi Zhou ◽  
Xi Sun ◽  
Charlotte Mobarak ◽  
A. Jay Gandolfi ◽  
Scott W. Burchiel ◽  
...  
Keyword(s):  
Arsenic Trioxide ◽  
Zinc Finger ◽  
Monomethylarsonous Acid ◽  
Differential Binding ◽  
Finger Peptides

Adjacent zinc-finger motifs in multiple zinc-finger peptides from SWI5 form structurally independent, flexibly linked domains

1992 ◽  
Vol 228 (2) ◽  
pp. 619-636 ◽  
Author(s):  
Yukinobu Nakaseko ◽  
David Neuhaus ◽  
Aaron Klug ◽  
Daniela Rhodes
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Motifs ◽  
Finger Peptides

Synthetic zinc finger peptides: old and novel applications

2004 ◽  
Vol 82 (4) ◽  
pp. 428-436 ◽  
Author(s):  
Nicoletta Corbi ◽  
Valentina Libri ◽  
Annalisa Onori ◽  
Claudio Passananti
Keyword(s):  
Gene Therapy ◽  
Zinc Finger ◽  
Chromatin Modification ◽  
Building Blocks ◽  
Artificial Transcription Factor ◽  
Finger Peptides ◽  
Finger Recognition ◽  
Novel Applications ◽  
Recognition Code ◽  
At Will

In the last decade, the efforts in clarifying the interaction between zinc finger proteins and DNA targets strongly stimulated the creativity of scientists in the field of protein engineering. In particular, the versatility and the modularity of zinc finger (ZF) motives make these domains optimal building blocks for generating artificial zinc finger peptides (ZFPs). ZFPs can act as transcription modulators potentially able to control the expression of any desired gene, when fused to an appropriate effector domain. Artificial ZFPs open the possibility to re-program the expression of specific genes at will and can represent a powerful tool in basic science, biotechnology and gene therapy. In this review we will focus on old, novel and possible future applications of artificial ZFPs.Key words: synthetic zinc finger, recognition code, artificial transcription factor, chromatin modification, gene therapy.

Complexes of zinc finger peptides with nickel(2+) and iron(2+)

1992 ◽  
Vol 31 (13) ◽  
pp. 2984-2986 ◽  
Author(s):  
Beth Allyn Krizek ◽  
Jeremy M. Berg
Keyword(s):  
Zinc Finger ◽  
Finger Peptides

Oxidation of Zn(Cys)4 Zinc Finger Peptides by O2 and H2O2: Products, Mechanism and Kinetics

2011 ◽  
Vol 17 (49) ◽  
pp. 13762-13772 ◽  
Author(s):  
Emilie Bourlès ◽  
Manon Isaac ◽  
Colette Lebrun ◽  
Jean-Marc Latour ◽  
Olivier Sénèque
Keyword(s):  
Zinc Finger ◽  
Mechanism And Kinetics ◽  
Finger Peptides

The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation

2010 ◽  
Vol 43 (1) ◽  
pp. 1-21 ◽  
Author(s):  
Aaron Klug
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Zinc Finger ◽  
Binding Proteins ◽  
Zinc Fingers ◽  
Dna Binding Proteins ◽  
Functional Domains ◽  
Control Of Gene Expression ◽  
Activation Domains ◽  
Finger Peptides

AbstractA long-standing goal of molecular biologists has been to construct DNA-binding proteins for the control of gene expression. The classical Cys2His2 (C2H2) zinc finger design is ideally suited for such purposes. Discriminating between closely related DNA sequences both in vitro and in vivo, this naturally occurring design was adopted for engineering zinc finger proteins (ZFPs) to target genes specifically.Zinc fingers were discovered in 1985, arising from the interpretation of our biochemical studies on the interaction of the Xenopus protein transcription factor IIIA (TFIIIA) with 5S RNA. Subsequent structural studies revealed its three-dimensional structure and its interaction with DNA. Each finger constitutes a self-contained domain stabilized by a zinc (Zn) ion ligated to a pair of cysteines and a pair of histidines and also by an inner structural hydrophobic core. This discovery showed not only a new protein fold but also a novel principle of DNA recognition. Whereas other DNA-binding proteins generally make use of the 2-fold symmetry of the double helix, functioning as homo- or heterodimers, zinc fingers can be linked linearly in tandem to recognize nucleic acid sequences of varying lengths. This modular design offers a large number of combinatorial possibilities for the specific recognition of DNA (or RNA). It is therefore not surprising that the zinc finger is found widespread in nature, including 3% of the genes of the human genome.The zinc finger design can be used to construct DNA-binding proteins for specific intervention in gene expression. By fusing selected zinc finger peptides to repression or activation domains, genes can be selectively switched off or on by targeting the peptide to the desired gene target. It was also suggested that by combining an appropriate zinc finger peptide with other effector or functional domains, e.g. from nucleases or integrases to form chimaeric proteins, genomes could be modified or manipulated.The first example of the power of the method was published in 1994 when a three-finger protein was constructed to block the expression of a human oncogene transformed into a mouse cell line. The same paper also described how a reporter gene was activated by targeting an inserted 9-base pair (bp) sequence, which acts as the promoter. Thus, by fusing zinc finger peptides to repression or activation domains, genes can be selectively switched off or on. It was also suggested that, by combining zinc fingers with other effector or functional domains, e.g. from nucleases or integrases, to form chimaeric proteins, genomes could be manipulated or modified.Several applications of such engineered ZFPs are described here, including some of therapeutic importance, and also their adaptation for breeding improved crop plants.

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