scholarly journals The Regulatory Role of RNA Metabolism Regulator TDP-43 in Human Cancer

2021 ◽  
Vol 11 ◽  
Author(s):  
Xueyou Ma ◽  
Yufan Ying ◽  
Haiyun Xie ◽  
Xiaoyan Liu ◽  
Xiao Wang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Human Cancer ◽  
Target Therapy ◽  
Dna Binding Protein ◽  
Rna Metabolism ◽  
Basic Knowledge ◽  
Tumor Target ◽  
Human Cancers ◽  
Rna And Dna

TAR-DNA-binding protein-43 (TDP-43) is a member of hnRNP family and acts as both RNA and DNA binding regulator, mediating RNA metabolism and transcription regulation in various diseases. Currently, emerging evidence gradually elucidates the crucial role of TDP-43 in human cancers like it is previously widely researched in neurodegeneration diseases. A series of RNA metabolism events, including mRNA alternative splicing, transport, stability, miRNA processing, and ncRNA regulation, are all confirmed to be closely involved in various carcinogenesis and tumor progressions, which are all partially regulated and interacted by TDP-43. Herein we conducted the first overall review about TDP-43 and cancers to systematically summarize the function and precise mechanism of TDP-43 in different human cancers. We hope it would provide basic knowledge and concepts for tumor target therapy and biomarker diagnosis in the future.

scholarly journals Role of the PEST sequence in the long-type GATA-6 DNA-binding protein expressed in human cancer cell lines

2012 ◽  
Vol 03 (04) ◽  
pp. 314-320 ◽  
Author(s):  
Kanako Obayashi ◽  
Kayoko Takada ◽  
Kazuaki Ohashi ◽  
Ayako Kobayashi-Ohashi ◽  
Masatomo Maeda
Keyword(s):  
Dna Binding ◽  
Cell Lines ◽  
Cancer Cell ◽  
Human Cancer ◽  
Dna Binding Protein ◽  
Cancer Cell Lines ◽  
Human Cancer Cell ◽  
Pest Sequence ◽  
Human Cancer Cell Lines

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.

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

scholarly journals FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein

Blood ◽  
2007 ◽  
Vol 110 (7) ◽  
pp. 2390-2398 ◽  
Author(s):  
Rigu Gupta ◽  
Sudha Sharma ◽  
Joshua A. Sommers ◽  
Mark K. Kenny ◽  
Sharon B. Cantor ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Single Stranded Dna

The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability.

scholarly journals Role of the Single-Stranded DNA–Binding Protein SsbB in Pneumococcal Transformation: Maintenance of a Reservoir for Genetic Plasticity

PLoS Genetics ◽  
2011 ◽  
Vol 7 (6) ◽  
pp. e1002156 ◽  
Author(s):  
Laetitia Attaiech ◽  
Audrey Olivier ◽  
Isabelle Mortier-Barrière ◽  
Anne-Lise Soulet ◽  
Chantal Granadel ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna

Post-ultraviolet DNA Synthesis in the Absence of Repair: Role of the Single-strand DNA-binding Protein

1989 ◽  
Vol 55 (5) ◽  
pp. 739-745 ◽  
Author(s):  
Ž. Trgovčević ◽  
N. Lerš ◽  
K. Brčić-Kostić ◽  
E. Salaj-Šmic
Keyword(s):  
Dna Binding ◽  
Dna Synthesis ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Strand
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