Cell cycle-dependent expression of nuclear matrix proteins of ehrlich ascites cells studied by in vitro translation

1986 ◽  
Vol 165 (1) ◽  
pp. 269-282 ◽  
Author(s):  
H. Bludau ◽  
M. Kopun ◽  
D. Werner
Keyword(s):  
Cell Cycle ◽  
Nuclear Matrix ◽  
Matrix Proteins ◽  
In Vitro Translation ◽  
Nuclear Matrix Proteins ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells ◽  
Cycle Dependent

Noncovalent Binding of Poly(ADP-Ribose) to Nuclear Matrix Proteins: Developmental Changes and Tissue Specificity

2000 ◽  
Vol 381 (11) ◽  
pp. 1047-1053 ◽  
Author(s):  
M. Malanga ◽  
B. Farina
Keyword(s):  
Nuclear Matrix ◽  
Noncovalent Interactions ◽  
Specific Protein ◽  
Noncovalent Interaction ◽  
Matrix Proteins ◽  
Nuclear Proteins ◽  
Rat Tissues ◽  
Nuclear Matrix Proteins

Abstract Poly(ADP-ribose) is a nuclear polynucleotide involved in the regulation of chromatin functions via covalent and/or noncovalent modification of nuclear proteins. Using a binding assay on protein blots, we searched for poly(ADP-ribose) binding proteins in nuclear matrices from testes of differently aged rats as well as from various adult rat tissues (brain, liver, spleen). We found that nuclear matrix proteins represent a significant subset of the nuclear proteins that can establish noncovalent interactions with poly(ADP-ribose). The profiles of poly(ADP-ribose) binding nuclear matrix proteins appeared to be tissue-specific and changed during postnatal development in the testis. The isolation and analysis of endogenous poly (ADP-ribose) from rat testes showed that the ADP-ribose polymers that bind nuclear matrix proteins in vitro are also present under physiologic conditions in vivo. These results further substantiate the possibility that poly(ADP-ribose) may affect chromatin functions through noncovalent interaction with specific protein targets, including nuclear matrix components.

In Vitro Heat Exposure Induces a Redistribution of Nuclear Matrix Proteins in Human K562 Erythroleukemia Cells

1994 ◽  
Vol 213 (1) ◽  
pp. 275-285 ◽  
Author(s):  
L.M. Neri ◽  
S. Santi ◽  
R.A. Marugg ◽  
B.M. Riederer ◽  
S. Capitani ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Heat Exposure ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Erythroleukemia Cells

scholarly journals MspI8, the repetitive sequence specifically interacting with nuclear matrix of rat testis cells.

1994 ◽  
Vol 41 (4) ◽  
pp. 459-466 ◽  
Author(s):  
J Rzeszowska-Wolny ◽  
J Rogoliński
Keyword(s):  
Nuclear Matrix ◽  
Gel Electrophoresis ◽  
Matrix Protein ◽  
Repetitive Sequences ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Rat Testis ◽  
The Matrix ◽  
Matrix Bound

The nuclear matrix bound DNA fraction of rat testis showed enrichment in repetitive sequences found in the 450 bp band after gel electrophoresis of the MspI digested rat DNA. DNA fragments isolated from this band were cloned. DNA of the clone pMspI8 showed homology to some representatives of rat LINE sequence family, and complexed in vitro more efficiently with testes nuclear matrix proteins than with yeast ARS1 sequence containing the matrix association region (MAR) or DNA from an other clone, MspI19. Western blot analysis showed that MspI8 sequence interacts with testes matrix protein of about 120 kDa.

CORTISOL-INDUCED PHOSPHORYLATION OF RAT LIVER NUCLEAR MATRIX PROTEINS IN IN VITRO SYSTEM

1981 ◽  
Vol 9 (2) ◽  
pp. 353P-353P
Author(s):  
Lj. Ševaljević ◽  
N. Brajanović ◽  
D. Trajković ◽  
K. Krtolica
Keyword(s):  
Rat Liver ◽  
Nuclear Matrix ◽  
Matrix Proteins ◽  
In Vitro System ◽  
Nuclear Matrix Proteins

ors12, a mammalian autonomously replicating DNA sequence, associates with the nuclear matrix in a cell cycle-dependent manner

1993 ◽  
Vol 105 (3) ◽  
pp. 807-818
Author(s):  
D.C. Mah ◽  
P.A. Dijkwel ◽  
A. Todd ◽  
V. Klein ◽  
G.B. Price ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Nuclear Matrix ◽  
Pcr Amplification ◽  
S Phase ◽  
Dependent Manner ◽  
The Matrix ◽  
S Period ◽  
Cycle Dependent

Origin enriched sequence ors8 and ors12, have been isolated previously by extrusion of nascent CV-1 cell DNA from replication bubbles at the onset of S-phase. Both have been shown to direct autonomous DNA replication in vivo and in vitro. Here, we have examined the association of genomic ors8 and ors12 with the nuclear matrix in asynchronous and synchronized CV-1 cells. In asynchronously growing cells, ors8 was found to be randomly distributed, while ors12 was found to be enriched on the nuclear matrix. Using an in vitro binding assay, we determined that ors12 contains two attachment sites, each located in AT-rich domains. Surprisingly, in early and mid-S-phase cells, ors12 homologous sequences were recovered mainly from the DNA loops, while in late-S the majority had shifted to positions on the nuclear matrix. In contrast, the distribution of ors8 over the matrix and loop DNA fractions did not change during the cell cycle. By bromodeoxyuridine substitution of replicating DNA, followed by immunoprecipitation with anti-bromodeoxyuridine antibodies and PCR amplification, we demonstrated that ors12 replicates almost exclusively on the matrix in early and mid-S-phase; replicating ors8 was also found to be enriched on the matrix in early S-phase. Chase experiments showed that the ors12 sequences labelled with bromodeoxyuridine in the first 2 hours of S-phase remain attached to the nuclear matrix, resulting in an accumulation of ors12 on the nuclear matrix at the end of the S period.

Differentiation-Specific Nuclear Matrix Proteins Cross-linked to DNA bycis-Diammine Dichloroplatinum

1998 ◽  
Vol 238 (1) ◽  
pp. 216-219 ◽  
Author(s):  
Elena Mattia ◽  
Margherita Eufemi ◽  
Silvia Chichiarelli ◽  
Mara Ceridono ◽  
Anna Ferraro
Keyword(s):  
Nuclear Matrix ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins

The Xenopus protein kinase pEg2 associates with the centrosome in a cell cycle-dependent manner, binds to the spindle microtubules and is involved in bipolar mitotic spindle assembly

1998 ◽  
Vol 111 (5) ◽  
pp. 557-572 ◽  
Author(s):  
C. Roghi ◽  
R. Giet ◽  
R. Uzbekov ◽  
N. Morin ◽  
I. Chartrain ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Mitotic Spindle ◽  
Cultured Cells ◽  
Dependent Manner ◽  
Egg Extracts ◽  
Pericentriolar Material ◽  
Spindle Microtubules ◽  
Cycle Dependent

By differential screening of a Xenopus laevis egg cDNA library, we have isolated a 2,111 bp cDNA which corresponds to a maternal mRNA specifically deadenylated after fertilisation. This cDNA, called Eg2, encodes a 407 amino acid protein kinase. The pEg2 sequence shows significant identity with members of a new protein kinase sub-family which includes Aurora from Drosophila and Ipl1 (increase in ploidy-1) from budding yeast, enzymes involved in centrosome migration and chromosome segregation, respectively. A single 46 kDa polypeptide, which corresponds to the deduced molecular mass of pEg2, is immunodetected in Xenopus oocyte and egg extracts, as well as in lysates of Xenopus XL2 cultured cells. In XL2 cells, pEg2 is immunodetected only in S, G2 and M phases of the cell cycle, where it always localises to the centrosomal region of the cell. In addition, pEg2 ‘invades’ the microtubules at the poles of the mitotic spindle in metaphase and anaphase. Immunoelectron microscopy experiments show that pEg2 is located precisely around the pericentriolar material in prophase and on the spindle microtubules in anaphase. We also demonstrate that pEg2 binds directly to taxol stabilised microtubules in vitro. In addition, we show that the presence of microtubules during mitosis is not necessary for an association between pEg2 and the centrosome. Finally we show that a catalytically inactive pEg2 kinase stops the assembly of bipolar mitotic spindles in Xenopus egg extracts.

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