scholarly journals RNAi-mediated downregulation of DNA binding protein A inhibits tumorigenesis in colorectal cancer

2016 ◽  
Vol 38 (3) ◽  
pp. 703-712 ◽  
Author(s):  
Rui-Ting Liu ◽  
Guo-Rong Wang ◽  
Chang Liu ◽  
Jian Qiu ◽  
Li-Kun Yan ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Dna Binding ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein

scholarly journals Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product.

1988 ◽  
Vol 170 (12) ◽  
pp. 5916-5918 ◽  
Author(s):  
R Aasland ◽  
J Coleman ◽  
A L Holck ◽  
C L Smith ◽  
C R Raetz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Gene Product ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein

scholarly journals The Up-Regulation of Y-Box Binding Proteins (DNA Binding Protein A and Y-Box Binding Protein-1) as Prognostic Markers of Hepatocellular Carcinoma

2005 ◽  
Vol 11 (20) ◽  
pp. 7354-7361 ◽  
Author(s):  
Mahmut Yasen ◽  
Kazunori Kajino ◽  
Sayaka Kano ◽  
Hiroshi Tobita ◽  
Junji Yamamoto ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Dna Binding ◽  
Binding Proteins ◽  
Prognostic Markers ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein

scholarly journals Highly repeated sites in the apolipoprotein(a) gene recognized by methylated DNA-binding protein, a sequence-specific DNA-binding protein.

1990 ◽  
Vol 10 (9) ◽  
pp. 4957-4960 ◽  
Author(s):  
K C Ehrlich ◽  
M Ehrlich
Keyword(s):  
Risk Factor ◽  
Dna Binding ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein ◽  
High Plasma ◽  
Methylated Dna ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
Lower Molecular Mass

Methylated DNA-binding protein (MDBP), a sequence-specific DNA-binding protein, was found to recognize more than 30 sites within an allele of the human apolipoprotein(a) gene. High plasma levels of apolipoprotein(a), a risk factor for atherosclerosis, have been correlated with genetically inherited lower-molecular-mass isoforms of this protein. MDBP might help down modulate the expression of the apolipoprotein(a) gene in a manner dependent on the length of a given allele of the gene and the number of MDBP sites in it.

scholarly journals The Bacteriophage T4 MotB Protein, a DNA-Binding Protein, Improves Phage Fitness

Viruses ◽  
2018 ◽  
Vol 10 (7) ◽  
pp. 343 ◽  
Author(s):  
Jennifer Patterson-West ◽  
Melissa Arroyo-Mendoza ◽  
Meng-Lun Hsieh ◽  
Danielle Harrison ◽  
Morgan Walker ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Bacteriophage T4 ◽  
Protein A ◽  
Dna Binding Protein

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 Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNA.

1997 ◽  
Vol 17 (4) ◽  
pp. 2194-2201 ◽  
Author(s):  
S D Miller ◽  
K Moses ◽  
L Jayaraman ◽  
C Prives
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Binding Protein ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Single Stranded Dna ◽  
C Terminus ◽  
P53 Response

Human replication protein A (RP-A) (also known as human single-stranded DNA binding protein, or HSSB) is a multisubunit complex involved in both DNA replication and repair. Potentially important to both these functions, it is also capable of complex formation with the tumor suppressor protein p53. Here we show that although p53 is unable to prevent RP-A from associating with a range of single-stranded DNAs in solution, RP-A is able to strongly inhibit p53 from functioning as a sequence-specific DNA binding protein when the two proteins are complexed. This inhibition, in turn, can be regulated by the presence of various lengths of single-stranded DNAs, as RP-A, when bound to these single-stranded DNAs, is unable to interact with p53. Interestingly, the lengths of single-stranded DNA capable of relieving complex formation between the two proteins represent forms that might be introduced through repair and replicative events. Increasing p53 concentrations can also overcome the inhibition by steady-state levels of RP-A, potentially mimicking cellular points of balance. Finally, it has been shown previously that p53 can itself be stimulated for site-specific DNA binding when complexed through the C terminus with short single strands of DNA, and here we show that p53 stays bound to these short strands even after binding a physiologically relevant site. These results identify a potential dual role for single-stranded DNA in the regulation of DNA binding by p53 and give insights into the p53 response to DNA damage.

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