What is the function of zinc finger nucleases?
Zinc finger nucleases (ZFNs) are a class of engineered DNA-binding proteins that facilitate targeted editing of the genome by creating double-strand breaks in DNA at user-specified locations.
What type of protein is zinc finger?
Zinc finger protein (ZFP) is a common DNA binding domain found in many transcription factors. It consists of ∼30 amino acids that may recognize three base pairs of DNA.
What does zinc do to proteins?
Not only is zinc required for essential catalytic functions in enzymes (more than 300 are known at present), but also it stabilizes and even induces the folding of protein subdomains.
Are zinc finger proteins transcription factors?
Zinc finger proteins are the largest transcription factor family in human genome. The diverse combinations and functions of zinc finger motifs make zinc finger proteins versatile in biological processes, including development, differentiation, metabolism and autophagy.
Why is it called zinc-finger?
Extended x-ray absorption fine structure confirmed the identity of the zinc ligands: two cysteines and two histidines. The DNA-binding loop formed by the coordination of these ligands by zinc were thought to resemble fingers, hence the name. Zinc fingers often bind to a sequence of DNA known as the GC box.
How are zinc finger nucleases made?
Zinc-finger nucleases (ZFNs) are artificial restriction enzymes generated by fusing a zinc finger DNA-binding domain to a DNA-cleavage domain. Zinc finger domains can be engineered to target specific desired DNA sequences and this enables zinc-finger nucleases to target unique sequences within complex genomes.
Where is zinc finger protein found?
The canonical members of this class contain a binuclear zinc cluster in which two zinc ions are bound by six cysteine residues. These zinc fingers can be found in several transcription factors including the yeast Gal4 protein.
How do zinc fingers recognize DNA?
Zinc fingers bind in the major groove of the DNA, wrapping around the strands, with specificity conferred by side chains of several amino acid on the α helices. Some zinc finger proteins undergo homodimerization by hydrophobic interactions or by finger-finger binding and reinforce the specific binding to DNA.
Why are zinc fingers called zinc fingers?
Can zinc fingers Dimerize?
The C2H2 zinc finger is the most prevalent protein motif in the mammalian proteome. We show here that these fingers comprise a bona fide dimerization domain.
Where are zinc-finger proteins found?
Znf domains are often found in clusters, where fingers can have different binding specificities. Znf motifs occur in several unrelated protein superfamilies, varying in both sequence and structure.
What is the function of the zinc finger protein?
The zinc finger antiviral protein (ZAP) is a cytoplasmic protein that confers a cell-autonomous protective effect against a variety of RNA viruses ( 2 ). Indeed, the replication of viruses as diverse as retroviruses, alphaviruses, filoviruses, and hepadnaviruses can be inhibited by ZAP ( 2 ⇓⇓ – 5 ).
Which is part of the Zap protein is required for antiviral function?
The ZAP protein includes an N-terminal ∼227-aa RNA-binding domain (RBD) containing 4 CCCH zinc fingers (ZnF1 to ZnF4), sometimes referred to as N-ZAP, that is necessary, and to some extent sufficient, for antiviral function ( 2, 6 ).
How is hzap able to bind to CG rich RNA?
Here, we determined a crystal structure of a protein-RNA complex containing the N-terminal, 4-zinc finger human (h) ZAP RNA-binding domain (RBD) and a CG dinucleotide-containing RNA target. The structure reveals in molecular detail how hZAP is able to bind selectively to CG-rich RNA.
What are the colors of the Zn ligand?
The UCG trinucleotide and the Zn ligands are shown in stick form with atomic colors (gray, C; red, O; blue, N; orange, P; yellow, S), and the Zn atoms are shown as gray spheres. We recently found that ZAP discriminates self from nonself (viral) RNAs based on their dinucleotide content ( 12 ).