Acidic Nucleoplasmic DNA-binding Protein (And-1) Controls Chromosome Congression by Regulating the Assembly of Centromere Protein A (CENP-A) at Centromeres

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.

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

Viruses ◽

10.3390/v10070343 ◽

2018 ◽

Vol 10 (7) ◽

pp. 343 ◽

Cited By ~ 3

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

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DNA binding protein A expression and methylation status in hepatocellular carcinoma and the adjacent tissue

International Journal of Oncology ◽

10.3892/ijo.2011.1282 ◽

2011 ◽

Author(s):

Mahmut Yasen

Keyword(s):

Hepatocellular Carcinoma ◽

Dna Binding ◽

Binding Protein ◽

Methylation Status ◽

Protein A ◽

Dna Binding Protein ◽

Adjacent Tissue

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Antimicrobial peptide LL-37 promotes the proliferation and invasion of skin squamous cell carcinoma by upregulating DNA-binding protein A

Oncology Letters ◽

10.3892/ol.2016.4865 ◽

2016 ◽

Vol 12 (3) ◽

pp. 1745-1752 ◽

Cited By ~ 7

Author(s):

Wei Wang ◽

Jinjing Jia ◽

Changji Li ◽

Qiqi Duan ◽

Jiao Yang ◽

...

Keyword(s):

Squamous Cell Carcinoma ◽

Dna Binding ◽

Antimicrobial Peptide ◽

Cell Carcinoma ◽

Squamous Cell ◽

Binding Protein ◽

Protein A ◽

Dna Binding Protein ◽

Skin Squamous Cell Carcinoma ◽

Proliferation And Invasion

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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 ◽

10.1182/blood-2006-11-057273 ◽

2007 ◽

Vol 110 (7) ◽

pp. 2390-2398 ◽

Cited By ~ 74

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.

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

Molecular and Cellular Biology ◽

10.1128/mcb.17.4.2194 ◽

1997 ◽

Vol 17 (4) ◽

pp. 2194-2201 ◽

Cited By ~ 28

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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