DNA Sequences Nonrandomly Distributed in Respect to Rat Liver Nuclear Matrix

1990 ◽  
pp. 333-336
Author(s):  
J. Rzeszowska-Wolny ◽  
J. Lanuszewska ◽  
J. Rogolinski
Keyword(s):  
Rat Liver ◽  
Dna Sequences ◽  
Nuclear Matrix

scholarly journals Dynamic associations of transcription factors with the rat liver nuclear matrix are functionally related to differential alpha-2-macroglobulin gene expression

2008 ◽  
Vol 60 (3) ◽  
pp. 355-366
Author(s):  
Svetlana Dinic ◽  
Mirjana Mihailovic ◽  
Svetlana Ivanovic-Matic ◽  
Aleksandra Uskokovic ◽  
Nevena Grdovic ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Rat Liver ◽  
Dna Sequences ◽  
Nuclear Matrix ◽  
Gene Promoter ◽  
Immunoblot Analysis ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Matrix Interactions ◽  
Gene Regulatory

Participation of the nuclear matrix in regulation of alpha-2-macroglobulin (?2M) gene transcription during rat liver development and the acute-phase (AP) response are examined. DNA affinity chromatography of fetal and adult liver internal nuclear matrix proteins under basal and AP conditions with the ?2M gene promoter (-852/+12) and immunoblot analysis revealed diverse patterns of association of transcription factors with the nuclear matrix. HNF-6, C/EBP?, and STAT5b were involved in basal and C/EBP?, STAT1, and STAT3 in AP-stimulated ?2M expression. These findings support the assumption that transcription factor-nuclear matrix interactions serve to channel gene regulatory proteins to DNA sequences.

Considerations in the isolation of rat liver nuclear matrix, nuclear envelope, and pore complex lamina

1981 ◽  
Vol 132 (1) ◽  
pp. 105-123 ◽  
Author(s):  
Scott H. Kaufmann ◽  
Donald S. Coffey ◽  
Joel H. Shaper
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Nuclear Matrix

scholarly journals DNA and proteins of the nuclear matrix are the main targets of benzo[a]pyrene's action in rat hepatocytes.

1993 ◽  
Vol 40 (4) ◽  
pp. 559-562 ◽  
Author(s):  
P Widłak ◽  
J Rzeszowska-Wolny
Keyword(s):  
Molecular Weight ◽  
Dna Adducts ◽  
Dna Sequences ◽  
Nuclear Matrix ◽  
Rat Hepatocytes ◽  
The Other ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Cultured Rat Hepatocytes ◽  
High Molecular Weight Proteins

The binding of [14C]benzo[a]pyrene (B[a]P) to DNA and proteins in total nuclei and subnuclear fractions of cultured rat hepatocytes was compared. The main targets of B[a]P were non-histone high molecular weight proteins of the nuclear matrix and DNA sequences attached to this structure. Following 24 h exposure to B[a]P the amounts of adducts in the nuclear matrix DNA and proteins were twice as high as in total nuclei. After withdrawal of the carcinogen containing medium the level of B[a]P-induced adducts gradually decreased but always remained the highest in the nuclear matrix proteins. Removal of adducts from the nuclear matrix DNA was more efficient than from the other DNA fractions, and 72 h after exposure to the carcinogen the level of DNA adducts in this fraction was similar to that in total nuclei.

scholarly journals A protein-tyrosine kinase in the nuclear matrix from rat liver

FEBS Letters ◽  
1986 ◽  
Vol 208 (2) ◽  
pp. 451-454 ◽  
Author(s):  
Yoshihisa Ohmura ◽  
Hirobumi Teraoka ◽  
Kinji Tsukada
Keyword(s):  
Tyrosine Kinase ◽  
Rat Liver ◽  
Nuclear Matrix ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine

scholarly journals Receptor binding in the rat liver nuclear matrix.

1986 ◽  
Vol 33 (5) ◽  
pp. 551-560 ◽  
Author(s):  
YUKIO SATOH ◽  
MASAO IZAWA ◽  
YOSHIKO HOSHIKAWA ◽  
SHOGO ICHII
Keyword(s):  
Rat Liver ◽  
Receptor Binding ◽  
Nuclear Matrix

ATPase and 5?-nucleotidase activity of rat liver nuclear matrix

1981 ◽  
Vol 91 (4) ◽  
pp. 531-533
Author(s):  
I. B. Bukhvalov ◽  
V. V. Delektorskaya ◽  
K. A. Perevoshchikova ◽  
I. B. Zbarskii ◽  
N. T. Raikhlin
Keyword(s):  
Rat Liver ◽  
Nuclear Matrix ◽  
Nucleotidase Activity

scholarly journals Boundary Element-Associated Factor 32B Connects Chromatin Domains to the Nuclear Matrix

2007 ◽  
Vol 27 (13) ◽  
pp. 4796-4806 ◽  
Author(s):  
Rashmi U. Pathak ◽  
Nandini Rangaraj ◽  
Satish Kallappagoudar ◽  
Krishnaveni Mishra ◽  
Rakesh K. Mishra
Keyword(s):  
Boundary Element ◽  
Dna Sequences ◽  
Nuclear Matrix ◽  
Domain Boundary ◽  
Coiled Coil ◽  
Boundary Elements ◽  
Structural Basis ◽  
Chromatin Domain ◽  
Eukaryotic Genomes

ABSTRACT Chromatin domain boundary elements demarcate independently regulated domains of eukaryotic genomes. While a few such boundary sequences have been studied in detail, only a small number of proteins that interact with them have been identified. One such protein is the boundary element-associated factor (BEAF), which binds to the scs′ boundary element of Drosophila melanogaster. It is not clear, however, how boundary elements function. In this report we show that BEAF is associated with the nuclear matrix and map the domain required for matrix association to the middle region of the protein. This region contains a predicted coiled-coil domain with several potential sites for posttranslational modification. We demonstrate that the DNA sequences that bind to BEAF in vivo are also associated with the nuclear matrix and colocalize with BEAF. These results suggest that boundary elements may function by tethering chromatin to nuclear architectural components and thereby provide a structural basis for compartmentalization of the genome into functionally independent domains.

scholarly journals Inactivation of 14-3-3ς Influences Telomere Behavior and Ionizing Radiation-Induced Chromosomal Instability

2000 ◽  
Vol 20 (20) ◽  
pp. 7764-7772 ◽  
Author(s):  
Sonu Dhar ◽  
Jeremy A. Squire ◽  
M. Prakash Hande ◽  
Raymund J. Wellinger ◽  
Tej K. Pandita
Keyword(s):  
Dna Sequences ◽  
Nuclear Matrix ◽  
Mammalian Cells ◽  
Eukaryotic Cell ◽  
Checkpoint Control ◽  
Aberrant Chromosome ◽  
M Phase ◽  
Chromosomal Breaks ◽  
Radiation Induced

ABSTRACT Telomeres are complexes of repetitive DNA sequences and proteins constituting the ends of linear eukaryotic chromosomes. While these structures are thought to be associated with the nuclear matrix, they appear to be released from this matrix at the time when the cells exit from G2 and enter M phase. Checkpoints maintain the order and fidelity of the eukaryotic cell cycle, and defects in checkpoints contribute to genetic instability and cancer. The 14-3-3ς gene has been reported to be a checkpoint control gene, since it promotes G2 arrest following DNA damage. Here we demonstrate that inactivation of this gene influences genome integrity and cell survival. Analyses of chromosomes at metaphase showed frequent losses of telomeric repeat sequences, enhanced frequencies of chromosome end-to-end associations, and terminal nonreciprocal translocations in 14-3-3ς−/− cells. These phenotypes correlated with a reduction in the amount of G-strand overhangs at the telomeres and an altered nuclear matrix association of telomeres in these cells. Since the p53-mediated G1 checkpoint is operative in these cells, the chromosomal aberrations observed occurred preferentially in G2 after irradiation with gamma rays, corroborating the role of the 14-3-3ς protein in G2/M progression. The results also indicate that even in untreated cycling cells, occasional chromosomal breaks or telomere-telomere fusions trigger a G2 checkpoint arrest followed by repair of these aberrant chromosome structures before entering M phase. Since 14-3-3ς−/− cells are defective in maintaining G2 arrest, they enter M phase without repair of the aberrant chromosome structures and undergo cell death during mitosis. Thus, our studies provide evidence for the correlation among a dysfunctional G2/M checkpoint control, genomic instability, and loss of telomeres in mammalian cells.

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