Bifunctional role of the zinc finger domains of the methyl-DNA-binding protein Kaiso

Evi-1 was originally identified as a common site of viral integration in murine myeloid tumors. Evi-1 encodes a 120-kDa polypeptide containing 10 zinc finger motifs located in two domains 380 amino acids apart and an acidic domain located carboxy terminal to the second set of zinc fingers. These features suggest that Evi-1 is a site-specific DNA-binding protein involved in the regulation of RNA transcription. We have purified Evi-1 protein from E. coli and have employed a gel shift-polymerase chain reaction method using random oligonucleotides to identify a high-affinity binding site for Evi-1. The consensus sequence for this binding site is TGACAAGATAA. Evi-1 protein specifically protects this motif from DNase I digestion. By searching the nucleotide sequence data bases, we have found this binding site both in sequences 5' to genes in putative or known regulatory regions and within intron sequences.

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PD104: An investigation of the role of a gene encoding a DNA binding protein in Treponema denticola

Journal Of Clinical Periodontology ◽

10.1111/jcpe.106_12914 ◽

2018 ◽

Vol 45 ◽

pp. 78-78

Keyword(s):

Dna Binding ◽

Binding Protein ◽

Dna Binding Protein ◽

Treponema Denticola ◽

Gene Encoding

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Role of UV-damaged DNA-binding protein-1 (DDB1) in early response to Pseudomonas syringae pv. tomato DC3000 infection in tomato

Canadian Journal of Plant Pathology ◽

10.1080/07060661.2018.1518930 ◽

2018 ◽

Vol 40 (4) ◽

pp. 562-570

Author(s):

Danfeng Zhang ◽

Junyang Yue ◽

Chenyan Hua ◽

Danyang Chen ◽

Yi Han ◽

...

Keyword(s):

Dna Binding ◽

Pseudomonas Syringae ◽

Binding Protein ◽

Early Response ◽

Dna Binding Protein ◽

Tomato Dc3000 ◽

Damaged Dna

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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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