Faculty Opinions recommendation of Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation.

2004 ◽  
Author(s):  
Philip Dawson
Keyword(s):  
Dna Binding ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Dna Binding Affinity

scholarly journals C-terminal in Sp1-like artificial zinc-finger proteins plays crucial roles in determining their DNA binding affinity

2013 ◽  
Vol 13 (1) ◽  
pp. 106 ◽  
Author(s):  
Baozhen Zhang ◽  
Shengyan Xiang ◽  
Yanru Yin ◽  
Liankun Gu ◽  
Dajun Deng
Keyword(s):  
Dna Binding ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Dna Binding Affinity

Multiconnection of Identical Zinc Finger: Implication for DNA Binding Affinity and Unit Modulation of the Three Zinc Finger Domain†

Biochemistry ◽  
2001 ◽  
Vol 40 (9) ◽  
pp. 2932-2941 ◽  
Author(s):  
Makoto Nagaoka ◽  
Tamaki Kaji ◽  
Miki Imanishi ◽  
Yuichiro Hori ◽  
Wataru Nomura ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Dna Binding Affinity

A SALL4 zinc finger missense mutation predicted to result in increased DNA binding affinity is associated with cranial midline defects and mild features of Okihiro syndrome

2006 ◽  
Vol 119 (1-2) ◽  
pp. 154-161 ◽  
Author(s):  
Jan Miertus ◽  
Wiktor Borozdin ◽  
Vladimir Frecer ◽  
Giorgio Tonini ◽  
Sara Bertok ◽  
...  
Keyword(s):  
Dna Binding ◽  
Missense Mutation ◽  
Binding Affinity ◽  
Zinc Finger ◽  
Midline Defects ◽  
Dna Binding Affinity

scholarly journals Lowering DNA binding affinity of SssI DNA methyltransferase does not enhance the specificity of targeted DNA methylation in E. coli

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Krystyna Ślaska-Kiss ◽  
Nikolett Zsibrita ◽  
Mihály Koncz ◽  
Pál Albert ◽  
Ákos Csábrádi ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Binding ◽  
Binding Affinity ◽  
Dna Methyltransferase ◽  
Restriction Enzymes ◽  
Dna Binding Protein ◽  
E Coli ◽  
Dna Binding Affinity ◽  
Higher Eukaryotes

AbstractTargeted DNA methylation is a technique that aims to methylate cytosines in selected genomic loci. In the most widely used approach a CG-specific DNA methyltransferase (MTase) is fused to a sequence specific DNA binding protein, which binds in the vicinity of the targeted CG site(s). Although the technique has high potential for studying the role of DNA methylation in higher eukaryotes, its usefulness is hampered by insufficient methylation specificity. One of the approaches proposed to suppress methylation at unwanted sites is to use MTase variants with reduced DNA binding affinity. In this work we investigated how methylation specificity of chimeric MTases containing variants of the CG-specific prokaryotic MTase M.SssI fused to zinc finger or dCas9 targeting domains is influenced by mutations affecting catalytic activity and/or DNA binding affinity of the MTase domain. Specificity of targeted DNA methylation was assayed in E. coli harboring a plasmid with the target site. Digestions of the isolated plasmids with methylation sensitive restriction enzymes revealed that specificity of targeted DNA methylation was dependent on the activity but not on the DNA binding affinity of the MTase. These results have implications for the design of strategies of targeted DNA methylation.

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