Swapping of the β-Hairpin Region between Sp1 and GLI Zinc Fingers:  Significant Role of the β-Hairpin Region in DNA Binding Properties of C2H2-type Zinc Finger Peptides†

Biochemistry ◽  
2005 ◽  
Vol 44 (7) ◽  
pp. 2523-2528 ◽  
Author(s):  
Yasuhisa Shiraishi ◽  
Miki Imanishi ◽  
Tatsuya Morisaki ◽  
Yukio Sugiura
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Significant Role ◽  
Zinc Fingers ◽  
Binding Properties ◽  
Finger Peptides ◽  
Dna Binding Properties

scholarly journals DNA Binding Properties of the Vitamin D3Receptor Zinc Finger Region

1991 ◽  
Vol 5 (12) ◽  
pp. 1815-1826 ◽  
Author(s):  
Leonard P. Freedman ◽  
Terri L. Towers
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Properties ◽  
Dna Binding Properties ◽  
Zinc Finger Region

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.

scholarly journals Expression, purification and DNA-binding properties of zinc finger domains of DOF proteins from Arabidopsis thaliana

Bioimpacts ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 167-176 ◽  
Author(s):  
Hakimeh Moghaddas Sani ◽  
Maryam Hamzeh-Mivehroud ◽  
Ana P. Silva ◽  
James L. Walshe ◽  
S. Abolghasem Mohammadi ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Dna Binding ◽  
Zinc Finger ◽  
Binding Properties ◽  
Zinc Finger Domains ◽  
Dna Binding Properties

scholarly journals The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide

2000 ◽  
Vol 44 (1) ◽  
pp. 295-296 ◽  
Author(s):  
Y. Hori ◽  
K. Suzuki ◽  
Y. Okuno ◽  
M. Nagaoka ◽  
S. Futaki ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Properties ◽  
Engineering Structure ◽  
Zinc Finger Peptide ◽  
Dna Binding Properties

scholarly journals Role of Advanced Glycation on Aggregation and DNA Binding Properties of α-Synuclein

2011 ◽  
Vol 24 (s2) ◽  
pp. 211-221 ◽  
Author(s):  
Vasudevaraju Padmaraju ◽  
Jamuna J. Bhaskar ◽  
Ummiti J.S. Prasada Rao ◽  
Paramahans V. Salimath ◽  
K.S. Rao
Keyword(s):  
Dna Binding ◽  
Advanced Glycation ◽  
Binding Properties ◽  
Dna Binding Properties
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