scholarly journals The Effect and Role of Carbon Atoms in Poly(β-amino ester)s for DNA Binding and Gene Delivery

2013 ◽  
Vol 135 (18) ◽  
pp. 6951-6957 ◽  
Author(s):  
Corey J. Bishop ◽  
Tiia-Maaria Ketola ◽  
Stephany Y. Tzeng ◽  
Joel C. Sunshine ◽  
Arto Urtti ◽  
...  
Keyword(s):  
Dna Binding ◽  
Gene Delivery ◽  
Amino Ester

Rapid Optimization of Gene Delivery by Parallel End-modification of Poly(β-amino ester)s

2007 ◽  
Author(s):  
Gregory T Zugates ◽  
Weidan Peng ◽  
Andreas Zumbuehl ◽  
Siddharth Jhunjhunwala ◽  
Yu-Hung Huang ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Amino Ester

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.

scholarly journals PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling

2021 ◽  
Vol 22 (10) ◽  
pp. 5112
Author(s):  
Lotte van Beek ◽  
Éilís McClay ◽  
Saleha Patel ◽  
Marianne Schimpl ◽  
Laura Spagnolo ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Parp Inhibitors ◽  
Covalent Modification ◽  
Activation Mechanism ◽  
Cancer Therapies ◽  
Damage Repair ◽  
Complementary Role ◽  
Functional Understanding

Poly (ADP-ribose) polymerases (PARP) 1-3 are well-known multi-domain enzymes, catalysing the covalent modification of proteins, DNA, and themselves. They attach mono- or poly-ADP-ribose to targets using NAD+ as a substrate. Poly-ADP-ribosylation (PARylation) is central to the important functions of PARP enzymes in the DNA damage response and nucleosome remodelling. Activation of PARP happens through DNA binding via zinc fingers and/or the WGR domain. Modulation of their activity using PARP inhibitors occupying the NAD+ binding site has proven successful in cancer therapies. For decades, studies set out to elucidate their full-length molecular structure and activation mechanism. In the last five years, significant advances have progressed the structural and functional understanding of PARP1-3, such as understanding allosteric activation via inter-domain contacts, how PARP senses damaged DNA in the crowded nucleus, and the complementary role of histone PARylation factor 1 in modulating the active site of PARP. Here, we review these advances together with the versatility of PARP domains involved in DNA binding, the targets and shape of PARylation and the role of PARPs in nucleosome remodelling.

scholarly journals Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding. VOLUME 280 (2005) PAGES 28382-28387

2006 ◽  
Vol 281 (50) ◽  
pp. 38966
Author(s):  
Takashi Kinebuchi ◽  
Wataru Kagawa ◽  
Hitoshi Kurumizaka ◽  
Shigeyuki Yokoyama
Keyword(s):  
Dna Binding ◽  
Terminal Domain

Role of the adenovirus 72-kDa DNA binding protein in the rapid decay of early viral mRNA

Virology ◽  
1988 ◽  
Vol 165 (2) ◽  
pp. 438-445 ◽  
Author(s):  
Ianis Lazaridis ◽  
Alexander Babich ◽  
Joseph R. Nevins
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Viral Mrna ◽  
Rapid Decay
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