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Identification of YY1 sequences necessary for association with the nuclear matrix and for transcriptional repression functions.

YY1 is a zinc finger-containing transcription factor that can both repress and activate transcription. YY1 appears to use multiple mechanisms to carry out its diverse functions. Recently, it was observed that YY1 can exist in multiple nuclear compartments. In addition to being present in the nuclear extract fraction, YY1 is also a component of the nuclear matrix. We show that YY1 can be sequestered in vivo into a high-molecular-weight complex and can be dislodged from this complex either by treatment with formamide or by incubation with an oligonucleotide containing the YY1 DNA binding site sequence. By transfecting plasmids expressing various YY1 deletion constructs and subsequent nuclear fractionation, we have identified sequences necessary for association with the nuclear matrix. These sequences (residues 256-340) co-localized with those necessary for in vivo sequestration of YY1 into the high-molecular-weight complex. We have also characterized YY1 sequences necessary for repression of activated transcription (residues 333-371) and those necessary for masking of the YY1 transactivation domain (residues 371-397). Sequences that repress activated transcription partially overlap YY1 sequences necessary for association with the nuclear matrix. However, these sequences are distinct from those that appear to mask the YY1 transactivation domain. The potential role of nuclear matrix association in controlling YY1 function is discussed.

3T3 Cells↗

Characterization of DNA pattern in the site of permanent attachment to the nuclear matrix located in the vicinity of replication origin.

The permanent sites of DNA attachment to the nuclear matrix in the domain of chicken alpha-globin genes originally found in erythrocyte nuclei have also been shown to exist in sperm and cultured fibroblast cells. A primary structure of a 1.7 kb fragment located in 5'-upstream region of chicken alpha-globin gene domain and containing both replication origin and permanent nuclear matrix attachment site has been determined. It was found to possess homologies with papovaviral replication origins and contain short internal repeats and GC-rich motifs.

Animals↗

[Phosphorylation of the nuclear matrix proteins of the liver and of Zajdela's hepatoma in the rat].

The rate of protein phosphorylation in isolated nuclear matrices from liver and Zajdela's hepatoma is very high, being even slightly higher than in isolated nuclei. This indicates that active protein kinases remain tightly bound to the nuclear matrix, since the areas of phosphorylation are the same. However, during isolation of the nuclear matrix from labeled nuclei in the absence of proteolysis and dephosphorylation inhibitors, most part of the label is eliminated from nuclear matrix proteins. These proteins were phosphorylated in both the tissues, however, in Zajdela's hepatoma, two proteins with a molecular weight of 29-31 kD and four proteins with a molecular weight of 12-19 kD were phosphorylated more intensely than in the liver.

Animals↗

Association of vitamin D receptors with the nuclear matrix of human and rat genitourinary tissues.

Calcitrol, 1,25 dihydroxyvitamin D3 (1,25-D3) has an important role in the antiproliferative and growth regulatory effects on normal and neoplastic cells (e.g. prostate cancer cells). 1,25-D3 binds to the vitamin D receptor (VDR), a member of the steroid receptor superfamily. Steroids, via intranuclear receptors, have been demonstrated to have high affinity binding to the nuclear matrix, the tissue specific scaffolding of the nucleus that is involved in the organization of DNA, replication and transcription. We hypothesized that the VDR interacts closely with the nuclear matrix in both human and rat tissues. In the studies described here, nuclear matrix proteins (NMP) were extracted from a number of rat and human tissues and immunoblot analysis performed using a rat anti-VDR antibody. The results from these studies reveal that the anti-VDR antibody detects six forms of the VDR in the NMP preparations: human testis demonstrated a protein of 57 and 52 kDa molecular weight compared with 57 and 37 kDa in the rat testis. Human prostate demonstrated proteins of 52 kDa compared to rat ventral (57 and 37 kDa) and dorsal prostate (52 and 26 kDa). Human and rat bladder NMP demonstrated a protein binding at 55 kDa and rat seminal vesicle NMP binding at 48 kDa. This is the first report of VDRs associated with the nuclear matrix. The varying molecular weight proteins reactive with the anti-VDR antibody within these tissues may represent different isoforms, proteolytic cleavage of a larger VDR or post-translational modification. The VDR-NMP interaction may be involved in the tissue specific actions of 1,25-D3 especially growth regulatory and antiproliferative effects.

Animals↗

Nuclear matrix localization of annexin V in chicken liver.

Fractionation of internal matrix proteins from chicken liver nuclei led to the isolation of a 32 kDa protein which was identified by partial amino acid sequence and immunological analysis as annexin V, an unreported nuclear matrix component. Our results showed that this protein is preferentially associated with the internal nuclear matrix fraction, since this is the only nuclear fraction where the protein can be immunodetected. Immunostaining on cultured cells also revealed a nuclear distribution with the exclusion of the nucleolar compartment and an association with cytosolic filamentous structures most likely corresponding to the cytoskeleton. Moreover, immunostaining on extracted cells to reveal the nuclear matrix showed a network-like distribution. Since annexin V has been reported as an inhibitor of protein kinase C, its nuclear localization in association with the internal matrix, which plays an important role in several nuclear processes, indicates its involvement in the regulation of signal transduction.

3T3 Cells↗

Specific organization of genes in relation to the sperm nuclear matrix.

We have recently reported that mammalian sperm DNA, the most highly condensed and functionally inert eukaryotic DNA, is organized into DNA loop domains attached at their bases to a sperm nuclear matrix (Chromosoma, 98: 153, 1989). We report here the specific arrangement of genes within the sperm loop domains by measuring the proximity of six hamster genes to the sperm nuclear matrix. After restriction endonuclease treatment of sperm nuclear matrices, five genes were clearly not associated with the sperm nuclear matrix and only one, alpha A-crystallin, was within 2 Kb of the matrix. This suggests that sperm DNA is organized in a specific manner in relation to the sperm matrix.

Animals↗

[The immunochemical demonstration of high-molecular proteins in the nuclear matrix of tumor cells].

For characterization of a high molecular-weight protein group prevailing in the tumor nuclear matrix, monoclonal antibodies to MAP-like protein p260 and to fibronectin were used. Immunoperoxidase reaction in Western blots of nuclear matrix electrophoregrams revealed protein p260 both in normal liver and hepatomas 27 and 22a while fibronectin was found in hepatomas, but absent in the normal liver. Immunoelectron microscopy with gold-conjugated antibodies showed p260 to be uniformly spread in the nuclei while fibronectin was localized mostly at the periphery of the tumour nuclei.

Animals↗

Chromosome territories, interchromatin domain compartment, and nuclear matrix: an integrated view of the functional nuclear architecture.

Advances in the specific fluorescent labeling of chromatin in fixed and living human cells in combination with three-dimensional (3D) and 4D (space plus time) fluorescence microscopy and image analysis have opened the way for detailed studies of the dynamic, higher-order architecture of chromatin in the human cell nucleus and its potential role in gene regulation. Several features of this architecture are now well established: 1. Chromosomes occupy distinct territories in the cell nucleus with preferred nuclear locations, although there is no evidence of a rigid suprachromosomal order. 2. Chromosome territories (CTs) in turn contain distinct chromosome arm domains and smaller chromatin foci or domains with diameters of some 300 to 800 nm and a DNA content in the order of 1 Mbp. 3. Gene-dense, early-replicating and gene-poor, middle-to-late-replicating chromatin domains exhibit different higher-order nuclear patterns that persist through all stages of interphase. In mitotic chromosomes early replicating chromatin domains give rise to Giemsa light bands, whereas middle-to-late-replicating domains form Giemsa dark bands and C-bands. In an attempt to integrate these experimental data into a unified view of the functional nuclear architecture, we present a model of a modular and dynamic chromosome territory (CT) organization. We propose that basically three nuclear compartments exist, an "open" higher-order chromatin compartment with chromatin domains containing active genes, a "closed" chromatin compartment comprising inactive genes, and an interchromatin domain (ICD) compartment (Cremer et al., 1993; Zirbel et al., 1993) that contains macromolecular complexes for transcription, splicing, DNA replication, and repair. Genes in "open," but not in "closed" higher-order chromatin compartments have access to transcription and splicing complexes located in the ICD compartment. Chromatin domains that build the "open" chromatin compartment are organized in a way that allows the direct contact of genes and nascent RNA to transcription and splicing complexes, respectively, preformed in the ICD compartment. In contrast, chromatin domains that belong to the "closed" compartment are topologically arranged and compacted in a way that precludes the accessibility of genes to transcription complexes. We argue that the content of the ICD compartment is highly enriched in DNA depleted biochemical matrix preparations. The ICD compartment may be considered as the structural and functional equivalent of the in vivo nuclear matrix. A matrix in this functional sense is compatible with but does not necessitate the concept of a 3D nuclear skeleton existing of long, extensively arborized filaments. In the absence of unequivocal evidence for such a structural matrix in the nucleus of living cells we keep an agnostic attitude about its existence and possible properties in maintaining the higher-order nuclear architecture. Quantitative modeling of the 3D and 4D human genome architecture in situ shows that such an assumption is not necessary to explain presently known aspects of the higher-order nuclear architecture. We expect that the interplay of quantitative modeling and experimental tests will result in a better understanding of the compartmentalized nuclear architecture and its functional consequences.

Animals↗

Human satellite 3 (HS3) binding protein from the nuclear matrix: isolation and binding properties.

Satellite DNA (satDNA) is the main component of residual DNA in nuclear matrix (NM) preparations. Gel mobility shift assay (GMSA) revealed specific human satellite 3 (HS3) binding activity in NM extracts. An HS3 binding protein was purified using diethylaminoethyl (DEAE)-cellulose and preparative GMSA. The binding was specific, although other satDNA fragments compete to some extent for the binding. DNase I footprinting and methylation interference revealed multiple points of protection distributed throughout the HS3 fragment with periodicity of about 10 bp, mostly inside an AT island. Polyclonal antibodies (AB) were raised against HS3-protein complexes cut from the preparative GMSA gel. On immunoblots, AB recognise a protein, which is not lamin, with apparent molecular mass 70 kDa, the same as revealed by purification (p70). In in situ nuclear matrix preparations combined immunofluorescence (AB) and fluorescent in situ hybridisation (HS3) shows that HS3 and p70 areas correspond to each other. The localisation of this protein detected with AB in interphase nuclei coincides with the heterochromatic regions which surround nucleoli in correspondence with the known HS3 position in the nuclei.

Antibodies↗

Structure of cytomatrix and nuclear matrix revealed by embedment-free electron microscopy.

Embedment-free electron microscopy (EFEM) is a new method which allows the visualisation of cytoskeleton in whole-mounted cells. In this study we employed EFEM to investigate the structure of cellular scaffolds in glioma C6 cell line. The cells were extracted with Triton X-100 that dissolves phospholipids in the membranes and removes most of cytoplasmic soluble proteins. The DNA and nuclear histones were removed with DNase I and high-salt buffer, respectively. The remaining cellular frameworks were temporary embedded in diethylene glycol distearate (DGD), sectioned and observed in transmission and scanning electron microscope after the removal of DGD. The predominant structure was the extensive meshwork of 10-20 nm filaments in the cytoplasm (cytomatrix) and 15-30 nm filaments in the nucleus (nuclear matrix). The 5 nm filaments, presumably corresponding to the actin filaments, were present in the cytomatrix, but not in the nuclear matrix. Moreover, the ultrathin (3 nm) filaments, connecting other cytoskeletal components were detected. Those are possibly identical with the previously described plectin filaments. For the first time we report the occurrence of ultrathin filaments in the nuclear matrix. Thus, in a addition to the well known cytoskeletal components (microtubules, intermediate filaments, actin microfilaments) EFEM showed a new type of filaments (the ultrathin filaments) in the cytomatrix and nuclear matrix. Further immunocytochemical studies are needed to determine the biochemical identity of the filaments observed in EFEM.

Animals↗

Interactions of rat repetitive sequence MspI8 with nuclear matrix proteins during spermatogenesis.

Using the Southwestern blot analysis we have studied the interactions between rat repetitive sequence MspI8 and the nuclear matrix proteins of rat testis cells. Starting from 2 weeks the young to adult animals showed differences in type of testis nuclear matrix proteins recognizing the MspI8 sequence. The same sets of nuclear matrix proteins were detected in some fractions enriched in spermatocytes and spermatides and obtained after fractionation of testis cells of adult animals by the velocity sedimentation technique.

Animals↗

Antibodies from patients with mixed connective tissue disease react with heterogeneous nuclear ribonucleoprotein or ribonucleic acid (hnRNP/RNA) of the nuclear matrix.

The sera of patients with mixed connective tissue disease (MCTD) have high titers of antibodies directed against nuclear U1-ribonucleoprotein (U1-RNP). This antigen is easily extracted from nuclear preparations with physiologic saline and from tissue sections with 0.1 HCl, leaving the nucleic acids and nuclear matrix behind. When U1-RNP is extracted from HEp-2 cells with 0.1 N HCl, the sera of 32/32 patients with MCTD react with another antigen that is exposed by the extraction procedure. This antigen is not destroyed by trypsin and deoxyribonuclease 1 treatment but is sensitive to both purified ribonuclease A and purified micrococcal nuclease. Absorption studies showed that the antibody reacting with this antigen cannot be absorbed by sheep red blood cells coated with extracts of rabbit thymus that contain U1-RNP. Radioimmunoassay showed that the reaction of the unadsorbed antibody was with heterogeneous nuclear ribonucleoprotein or ribonucleic acid (hnRNP/RNA) and not with transfer RNA or ribosomal RNA. The hnRNP/RNA antigen is demonstrated as discrete particles in the internucleolar chromatin of interphase cells, but in metaphase cells the antigen is diffusely dispersed. The distribution, solubility, and biochemical characteristics suggest that the antigenic moiety is part of the nuclear matrix. Therefore, MCTD sera contain antibodies that react with at least two species of nuclear RNP: small nuclear RNP (snRNP), as described by others, and a high m.w. hnRNP/RNA bound to the nuclear matrix.

Animals↗

A DNA-binding element for a steroid receptor-binding factor is flanked by dual nuclear matrix DNA attachment sites in the c-myc gene promoter.

The receptor-binding factor (RBF) for the avian oviduct progesterone (Pg) receptor (PR) has previously been shown to be a unique 10-kDa nuclear matrix protein that generates high affinity PR-binding sites on avian DNA. This paper describes the use of Southwestern blot and DNA gel shift analyses with RBF protein to identify a minimal 54-base pair RBF-binding element in the matrix-associated region (MAR) of the Pg-regulated c-myc gene promoter. This element contains a 5'-GC-rich domain and a 3'-AT-rich domain, the latter of which has a homopurine/homopyrimidine structure. The gel shift assays required the generation of an RBF-maltose fusion protein (RBF-MBP), which specifically binds this element and is supershifted when the anti-RBF polyclonal antibody is added. Computer analysis of the full-length amino acid sequence for RBF predicts a DNA-binding motif involving a beta-sheet structure at the N-terminal domain. Southern blot analyses using nuclear matrix DNA suggests that there are dual MAR sites in the c-myc promoter, which flank an intervening domain containing the RBF element. The co-transfection of this MAR sequence, containing the RBF element and cloned into a luciferase reporter vector, together with an RBF expression vector construct, into steroid treated human MCF-7 cells, results in a decrease of the c-myc promoter activity relative to control transfections containing only the parent vector of the RBF expression construct. These data suggest that a unique chromatin/nuclear matrix structure, composed of the RBF-DNA element complex which is flanked by nuclear matrix attachment sites, serves to bind the PR and repress the c-myc promoter.

Animals↗

The effect of sodium tetrathionate stabilization on the distribution of three nuclear matrix proteins in human K562 erythroleukemia cells.

Using both conventional fluorescence and confocal laser scanning microscopy we have investigated whether or not stabilization of isolated human erythroleukemic nuclei with sodium tetrathionate can maintain in the nuclear matrix the same spatial distribution of three polypeptides (M(r) 160 kDa and 125 kDa, previously shown to be components of the internal nuclear matrix plus the 180-kDa nucleolar isoform of DNA topoisomerase II) as seen in permeabilized cells. The incubation of isolated nuclei in the presence of 2 mM sodium tetrathionate was performed at 0 degrees C or 37 degrees C. The matrix fraction retained 20-40% of nuclear protein, depending on the temperature at which the chemical stabilization was executed. Western blot analysis revealed that the proteins studied were completely retained in the high-salt resistant matrix. Indirect immunofluorescence experiments showed that the distribution of the three antigens in the final matrix closely resembled that detected in permeabilized cells, particularly when the stabilization was performed at 37 degrees C. This conclusion was also strengthened by analysis of cells, isolated nuclei and the nuclear matrix by means of confocal laser scanning microscopy. We conclude that sodium tetrathionate stabilization of isolated nuclei does not alter the spatial distribution of some nuclear matrix proteins.

Blotting, Western↗

Changes in nuclear matrix proteins during the senescence-like phenomenon induced by 5-chlorodeoxyuridine in HeLa cells.

5-Chlorodeoxyuridine (CldU) immediately induces a senescence-like phenomenon in any type of mammalian cells probably due to a change in nuclear matrix structure. We thus examined nuclear matrix proteins in HeLa cells cultured with CldU by high-resolution two-dimensional gel electrophoresis and peptide mass spectrometry. Three proteins were found to be down-regulated and one protein up-regulated by addition of CldU. In addition, one acidic protein accumulated in the nuclear matrix, although not quantitatively changed in the nuclei. Since these alterations were observed within 24h after addition of CldU, these proteins may be involved in an early step of the senescence-like phenomenon.

Antigens, Nuclear↗

[The intermediate filament-lamina-nuclear matrix system of ES-M13 cells].

Sequential extraction and DGD embedment-free section TEM techniques were used as new methods to study the intermediate filament-lamina-nuclear matrix (IF-L-NM) system of cells. Murine embryonic stem cells (ES-M13) were investigated by means of electron microscopy, immunofluorescence microscopy and Western-blot analysis. There existed a delicate nuclear matrix network in the nucleus domain of detergent-extracted ES cells. The filaments of the nuclear matrix were found in close association with the nuclear lamina. Some intermediate filaments were also observed in the cytoplasm. In immunofluorescence microscopy, a bright, slightly granular cytoplasmic fluorescence, showing no polar concentration, was revealed with keratin monoclonal antibody AF5. We could not detect any significant fibrillar staining in the ES cells by indirect immunofluorescence method. With antibodies to vimentin and desmin, the ES cells showed only a nonspecific, weak fluorescence, similar to that seen in the control. In Western-blot analysis of electrophoretically separated polypeptides, three polypeptides with molecular weight of 65 KD, 62 KD and 52 KD, reactive with keratin monoclonal antibody were detected in the ES cells.

Animals↗

Association of actin with DNA and nuclear matrix from Guerin ascites tumour cells.

The protein composition of nuclear matrices containing different amount of DNA was examined. It was found that, in matrices containing 2% to 80% of total DNA, the quantity of DNA-bound proteins remains relatively constant varying from 10% to 15% of total nuclear proteins. Electrophoretic patterns do not differ substantially, but autoradiograms with in vitro 125I labelled proteins show quantitative variations in the actin content. Application of radioimmunoassay (RIA) enabled to determine the exact content of actin in GAT nuclei and nuclear matrices - 5 micrograms/ml in nuclei, of which 50% are bound to DNA and 30% being a component of the protein part of the nuclear matrix. These results are supported by electron microscopic data, where immunogold technique was performed on thin sections and spread material. The applied methods suggest that part of the nuclear actin is tightly bound (resistant to 2 M NaCl) to DNA and represents a component of the internal nuclear matrix.

Actins↗

The association of HPV 16 DNA with specific nuclear matrix proteins of normal and cervical carcinoma cell.

Human papillomavirus type 16 (HPV 16) has been found to be integrated into the DNA of epithelial cells in most cervical cancers. The HPV16 DNA is bound to different nuclear matrix proteins in normal and cervical carcinoma cells. It has high affinity, for acidic proteins in cancer cells. The molecular weights of the acidic proteins are 200 kD, 186 kD and 67 kD. On the other hand, the viral DNA seemed to bind to higher molecular weight basic nuclear matrix proteins (250 kD, 150 kD) of normal cells. Further investigation of the functional roles of these nuclear matrix proteins may provide insight into the process of carcinogenesis of the cervix.

DNA, Viral↗