A tissue-specific MAR SAR DNA-binding protein with unusual binding site recognition

@article{Dickinson1992AT,
  title={A tissue-specific 
                  
                     
                        MAR
                     
                     
                        SAR
                     
                  
                DNA-binding protein with unusual binding site recognition },
  author={Liliane A. Dickinson and Tadashi Joh and Yoshinori Kohwi and Terumi Kohwi-Shigematsu},
  journal={Cell},
  year={1992},
  volume={70},
  pages={631-645}
}
A Novel Matrix Attachment Region DNA Binding Motif Identified Using a Random Phage Peptide Library (*)
TLDR
Phage display may provide a general tool for rapid identification of DNA binding peptide motifs and show that a nine amino acid sequence in SATB1 represents a key MAR binding motif.
Nucleolin is a matrix attachment region DNA-binding protein that specifically recognizes a region with high base-unpairing potential
TLDR
Nucleolin effectively distinguishes between a double-stranded wild-type synthetic MAR sequence with a high base-unpairing potential and its mutated version that has lost the unpairing capability but is still A+T rich.
The regulatory element 3' to the A gamma-globin gene binds to the nuclear matrix and interacts with special A-T-rich binding protein 1 (SATB1), an SAR/MAR-associating region DNA binding protein.
TLDR
Binding of SATB1 to two sites within the 3' A gamma regulatory element and its MAR/SAR activity suggests that this element may influence gene expression through interaction with the nuclear matrix.
Nuclear matrix protein ARBP recognizes a novel DNA sequence motif with high affinity.
TLDR
The results indicate that ARBP recognizes a novel DNA sequence motif containing the central sequence 5'-GGTGT-3' and flanking AT-rich sequences andStructural elements of the sequence motif are probably also recognized.
The combination of sequence-specific and nonspecific DNA-binding modes of transcription factor SATB1.
TLDR
It is believed that the lack of highly conserved basic residues in the helix relevant to the base recognition loosens its fitting into the DNA groove and impairs the specific binding, and the combination of the sequence-specific and nonspecific DNA-binding modes of SATB1 should be advantageous in a search for target loci during transcriptional regulation.
PDZ domain-mediated dimerization and homeodomain-directed specificity are required for high-affinity DNA binding by SATB1
TLDR
A model for SATB1–DNA complex in which the HDs bind in an antiparallel fashion to the palindromic consensus element via minor groove, bridged by the PDZ-like dimerization domain is proposed.
Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB 1
TLDR
A significant number of equivalent contacts are observed for typically four-helix POU-specific domains of POUhomologous proteins, indicating that these domains share a common framework of the DNA-binding mode, recognizing partially similar DNA sequences.
An Atypical Homeodomain in SATB1 Promotes Specific Recognition of the Key Structural Element in a Matrix Attachment Region*
TLDR
Site-directed mutagenesis of the core unwinding element in the 3′ MAR of the immunoglobulin heavy chain gene enhancer revealed the sequence 5′-(C/A)TAATA-3′ to be essential for the increase in affinity mediated by the homeodomain.
A Large DNA-binding Nuclear Protein with RNA Recognition Motif and Serine/Arginine-rich Domain (*)
TLDR
Human NP220 is a novel type of nucleoplasmic protein with multiple domains that binds to double-stranded DNA fragments by recognizing clusters of cytidines and has an arginine/serine-rich domain commonly found in pre-mRNA splicing factors.
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TLDR
Avian nuclear matrices are examined for the presence of very tight cellular DNA-protein complexes in the region of the beta-globin gene enhancer and of several other avian genes to suggest certain regions of cellular DNA are very tightly, perhaps covalently, attached to nuclear matrix-associated proteins.
A mammalian high mobility group protein recognizes any stretch of six A.T base pairs in duplex DNA.
TLDR
Findings indicate that, rather than binding to a few specific DNA sequences, alpha-protein recognizes a configuration of the minor groove characteristic of short runs of A X T base pairs.
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TLDR
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TLDR
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TLDR
A new technique for quickly determining which nucleosides in a DNA molecule are contacted by a sequence-specific DNA-binding protein is reported, and the missing nucleoside data show that the amino-terminal arms of lambda repressor make energetically important contacts with positions 7 and 8 and the central dyad base pair of the operator.
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We have used a recombinant bacteriophage that expresses the DNA-binding domain of C/EBP to optimize conditions for a screening technique that may facilitate the cloning of genes that encode
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