Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

1999 ◽  
Vol 11 (6) ◽  
pp. 1117
Author(s):  
Frank Gindullis ◽  
Iris Meier
Keyword(s):  
Nuclear Envelope ◽  
Binding Protein ◽  
Matrix Attachment Region ◽  
Attachment Region ◽  
Discrete Domains

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.

Characterisation and high-resolution distribution of a matrix attachment region-binding protein (MFP1) in proliferating cells of onion

Planta ◽  
2001 ◽  
Vol 212 (4) ◽  
pp. 535-546 ◽  
Author(s):  
Rafael Samaniego ◽  
Wendou Yu ◽  
Iris Meier ◽  
Susana Moreno Díaz de la Espina
Keyword(s):  
High Resolution ◽  
Binding Protein ◽  
Matrix Attachment Region ◽  
Proliferating Cells ◽  
Attachment Region

scholarly journals Nucleolin is a matrix attachment region DNA-binding protein that specifically recognizes a region with high base-unpairing potential.

1995 ◽  
Vol 15 (1) ◽  
pp. 456-465 ◽  
Author(s):  
L A Dickinson ◽  
T Kohwi-Shigematsu
Keyword(s):  
Binding Protein ◽  
K562 Cells ◽  
Matrix Attachment Region ◽  
Affinity Column ◽  
Rrna Gene ◽  
Wild Type ◽  
The Matrix ◽  
Attachment Region ◽  
Nuclear Matrix Attachment Region ◽  
High Base

A DNA affinity column containing a synthetic double-stranded nuclear matrix attachment region (MAR) was used to purify a 100-kDa protein from human erythroleukemia K562 cells. This protein was identified as nucleolin, the key nucleolar protein of dividing cells, which is thought to control rRNA gene transcription and ribosome assembly. Nucleolin is known to bind RNA and single-stranded DNA. We report here that nucleolin is also a MAR-binding protein. It binds double-stranded MARs from different species with high affinity. 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. Thus, nucleolin is not merely an A+T-rich sequence-binding protein but specifically binds the base-unpairing region of MARs. This binding specificity is similar to that of the previously cloned tissue-specific MAR-binding protein SATB1. Unlike SATB1, which binds only double-stranded MARs, nucleolin binds the single-stranded T-rich strand of the synthetic MAR probe approximately 45-fold more efficiently than its complementary A-rich strand, which has an affinity comparable to that of the double-stranded form of the MAR. In contrast to the high selectivity of binding to double-stranded MARs, nucleolin shows only a small but distinct sequence preference for the T-rich strand of the wild-type synthetic MAR over the T-rich strand of its mutated version. The affinity to the T-rich synthetic MAR is severalfold higher than to its corresponding RNA and human telomere DNA. Quantitative cellular fractionation and extraction experiments indicate that nucleolin is present both as a soluble protein and tightly bound to the matrix, similar to other known MAR-binding proteins.

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