scholarly journals Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1

2007 ◽  
Vol 35 (15) ◽  
pp. 5073-5084 ◽  
Author(s):  
Kazuhiko Yamasaki ◽  
Toshihiko Akiba ◽  
Tomoko Yamasaki ◽  
Kazuaki Harata
Keyword(s):  
Transcription Factor ◽  
Matrix Attachment Region ◽  
Structural Basis ◽  
The Matrix ◽  
Attachment Region

scholarly journals Screening of a Protein That Interacts with the Matrix Attachment Region-Binding Protein fromDunaliella salina

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Rui Yang ◽  
Zhaoxi Li ◽  
Yan Lin ◽  
Baosheng Yang ◽  
Tianyun Wang
Keyword(s):  
Binding Protein ◽  
Matrix Attachment Region ◽  
Regulatory Function ◽  
Glutathione S Transferase ◽  
Reading Frame ◽  
Cis Acting ◽  
Binding Partner ◽  
The Matrix ◽  
Attachment Region ◽  
Regulated Functions

We isolated the matrix attachment region-binding protein (MBP) DMBP-1 fromDunaliella salinain our previous studies. MBPs are part of the cis-acting protein family cluster. The regulatory function possibly works through the interaction of the MBPs with each other. In the present study, DMBP-1 was used as the bait in screening theD. salinacDNA library for DMBP-1 interactors that could potentially mediate the DMBP-1-regulated functions. A novel MBP, namely, DMBP-2, was identified as a DMBP-1 binding partner. The cDNA of DMBP-1 was 823 bp long and contained a 573 bp open reading frame, which encoded a polypeptide of 191 amino acids. The interaction between DMBP-2 and DMBP-1 was further confirmed through glutathione S-transferase pull-down assays.

scholarly journals Interactions of the matrix attachment region of DNA with the matrix proteins from the copper preincubated liver nuclei.

1995 ◽  
Vol 42 (2) ◽  
pp. 205-210 ◽  
Author(s):  
P Widłak ◽  
J Rogoliński ◽  
J Rzeszowska-Wolny
Keyword(s):  
Rat Liver ◽  
Copper Ions ◽  
Specific Interaction ◽  
Protein Composition ◽  
Matrix Proteins ◽  
Matrix Attachment Region ◽  
The Matrix ◽  
Attachment Region ◽  
Liver Nuclei ◽  
The Stability

Preincubation of rat liver nuclei with copper ions influenced the stability and protein composition of the nuclear matrices isolated by a "high salt" method. Also the specific interaction between matrix proteins and the kappa Ig matrix attachment region of DNA was affected.

Sequence rearrangement in the AT-rich minisatellite of the novel rice transposable element Basho

Genome ◽  
2002 ◽  
Vol 45 (3) ◽  
pp. 493-502 ◽  
Author(s):  
Tsuyoshi Inukai ◽  
Yoshio Sano
Keyword(s):  
Repeat Unit ◽  
Rice Genome ◽  
Single Strand ◽  
Homology Search ◽  
Matrix Attachment Region ◽  
Site Preference ◽  
The Matrix ◽  
Attachment Region ◽  
Flanking Sequences ◽  
Direct Amplification

In the process of characterizing a rice wx deletion mutant, an AT-rich minisatellite sequence that consisted of units of ~80 bp was detected about 2.3 kb downstream of the wx gene. This AT-rich minisatellite was a multiple-copy element (1 × 103 to 2 × 103 copies per haploid genome) and interspersed in the rice genome. By BLAST homology search it was indicated that not only the tandem repeat but also both flanking sequences were conserved among copies. According to the characteristics of the termini (5'-CHH ...CTAG-3') and a target site preference for T, this AT-rich minisatellite accompanying the flanking sequences was classified into a novel transposon, Basho. The results of direct amplification of Basho showed that relatively large variation in size existed in the Basho family. We estimate the variation to be generated by not only alteration of the number of units in the minisatellite but also by duplications of larger blocks including the conserved flanking sequences caused by single-strand mispairing (SSM) at noncontiguous repeats. Because the AT-rich minisatellite contained in Basho possessed several motifs of the matrix attachment region (MAR) in its repeat unit, the functional role as MAR in the rice genome was discussed.Key words: Oryza sativa, minisatellite, Basho, single strand mispairing (SSM).

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