Delineation of Methyl-DNA Binding Protein Interactions in the Prostate Cancer Genome

2013 ◽  
Author(s):  
Roderick T. Hori
Keyword(s):  
Prostate Cancer ◽  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Cancer Genome

A new visible-light-driven photoelectrochemical biosensor for probing DNA–protein interactions

2015 ◽  
Vol 51 (39) ◽  
pp. 8381-8384 ◽  
Author(s):  
Zheng-Yuan Ma ◽  
Yi-Fan Ruan ◽  
Nan Zhang ◽  
Wei-Wei Zhao ◽  
Jing-Juan Xu ◽  
...  
Keyword(s):  
Dna Binding ◽  
Visible Light ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Visible Light Driven ◽  
Photoelectrochemical Biosensor ◽  
Dna Protein Interactions

A novel photoelectrochemical approach was achieved for the detection of a DNA binding protein via the protein–DNA interaction.

scholarly journals The role of chromodomain helicase DNA binding protein 1 (CHD1) in promoting an invasive prostate cancer phenotype

2021 ◽  
Vol 13 ◽  
pp. 175628722110224
Author(s):  
Aparna Kareddula ◽  
Daniel J. Medina ◽  
Whitney Petrosky ◽  
Sonia Dolfi ◽  
Irina Tereshchenko ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Dna Binding ◽  
Adhesion Molecules ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Matrix Metalloproteinase 2 ◽  
Epithelial Cell Line ◽  
Target Cells ◽  
Integrin Subunit ◽  
Suspension Cells

Background: Prostate cancer (PCa) phenotypes vary from indolent to aggressive. Molecular subtyping may be useful in predicting aggressive cancers and directing therapy. One such subtype involving deletions of chromodomain helicase DNA binding protein 1 ( CHD1), a tumor suppressor gene, are found in 10–26% of PCa tumors. In this study, we evaluate the functional cellular effects that follow CHD1 deletion. Methods: CHD1 was knocked out (KO) in the non-tumorigenic, human papillomavirus 16 (HPV16)-immortalized prostate epithelial cell line, RWPE-1, using CRISPR/Cas9. In vitro assays such as T7 endonuclease assay, western blot, and sequencing were undertaken to characterize the CHD1 KO clones. Morphologic and functional assays for cell adhesion and viability were performed. To study expression of extracellular matrix (ECM) and adhesion molecules, a real-time (RT) profiler assay was performed using RWPE-1 parental, non-target cells (NT2) and CHD1 KO cells. Result: Compared to parental RWPE-1 and non-target cells (NT2), the CHD1 KO cells had a smaller, rounder morphology and were less adherent under routine culture conditions. Compared to parental cells, CHD1 KO cells showed a reduction in ECM and adhesion molecules as well as a greater proportion of viable suspension cells when cultured on standard tissue culture plates and on plates coated with laminin, fibronectin or collagen I. CHD1 KO cells showed a decrease in the expression of secreted protein acidic and rich in cysteine (SPARC), matrix metalloproteinase 2 (MMP2), integrin subunit alpha 2 (ITGA2), integrin subunit alpha 5 (ITGA5), integrin subunit alpha 6 (ITGA6), fibronectin (FN1), laminin subunit beta-3 precursor (LAMB3), collagen, tenascin and vitronectin as compared to parental and NT2 cells. Conclusion: These data suggest that in erythroblast transformation specific (ETS) fusion-negative, phosphatase and tensin homolog ( PTEN) wildtype PCa, deletion of CHD1 alters cell-cell and cell-matrix adhesion dynamics, suggesting an important role for CHD1 in the development and progression of PCa.

Protein-Protein Interactions between the Escherichia coli Single-Stranded DNA-Binding Protein and Exonuclease I

1996 ◽  
Vol 145 (5) ◽  
pp. 619 ◽  
Author(s):  
Margarita Sandigursky ◽  
Frances Mendez ◽  
Robert E. Bases ◽  
Tomohiro Matsumoto ◽  
William A. Franklin
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Exonuclease I

scholarly journals High Expression of KIF22/Kinesin-Like DNA Binding Protein (Kid) as a Poor Prognostic Factor in Prostate Cancer Patients

2018 ◽  
Vol 24 ◽  
pp. 8190-8197 ◽  
Author(s):  
Zheng Zhang ◽  
Hui Xie ◽  
Shimiao Zhu ◽  
Xuanrong Chen ◽  
Jianpeng Yu ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Prognostic Factor ◽  
Dna Binding ◽  
Cancer Patients ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
High Expression ◽  
Poor Prognostic Factor

scholarly journals Frequent Disruption of Chromodomain Helicase DNA-Binding Protein 8 (CHD8) and Functionally Associated Chromatin Regulators in Prostate Cancer

Neoplasia ◽  
2014 ◽  
Vol 16 (12) ◽  
pp. 1018-1027 ◽  
Author(s):  
Nathan A. Damaschke ◽  
Bing Yang ◽  
Michael L. Blute ◽  
Chee Paul Lin ◽  
Wei Huang ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Chromatin Regulators

scholarly journals Studies of the Interaction between Rad52 Protein and the Yeast Single-Stranded DNA Binding Protein RPA

1998 ◽  
Vol 18 (7) ◽  
pp. 4400-4406 ◽  
Author(s):  
Sharon L. Hays ◽  
Antoine A. Firmenich ◽  
Philip Massey ◽  
Ronadip Banerjee ◽  
Paul Berg
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Large Subunit ◽  
Critical Role ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Mutant Proteins ◽  
Two Hybrid

ABSTRACT The RFA1 gene encodes the large subunit of the yeast trimeric single-stranded DNA binding protein replication protein A (RPA), which is known to play a critical role in DNA replication. ASaccharomyces cerevisiae strain carrying therfa1-44 allele displays a number of impaired recombination and repair phenotypes, all of which are suppressible by overexpression of RAD52. We demonstrate that a rad52 mutation is epistatic to the rfa1-44 mutation, placingRFA1 and RAD52 in the same genetic pathway. Furthermore, two-hybrid analysis indicates the existence of interactions between Rad52 and all three subunits of RPA. The nature of this Rad52-RPA interaction was further explored by using two different mutant alleles of rad52. Both mutations lie in the amino terminus of Rad52, a region previously defined as being responsible for its DNA binding ability (U. H. Mortenson, C. Beudixen, I. Sunjeuaric, and R. Rothstein, Proc. Natl. Acad. Sci. USA 93:10729–10734, 1996). The yeast two-hybrid system was used to monitor the protein-protein interactions of the mutant Rad52 proteins. Both of the mutant proteins are capable of self-interaction but are unable to interact with Rad51. The mutant proteins also lack the ability to interact with the large subunit of RPA, Rfa1. Interestingly, they retain their ability to interact with the medium-sized subunit, Rfa2. Given the location of the mutations in the DNA binding domain of Rad52, a model incorporating the role of DNA in the protein-protein interactions involved in the repair of DNA double-strand breaks is presented.

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