Activated murine α-globin gene is not preferentially associated with the nuclear matrix

Kirov, N.; Tsanev, Roumen

doi:10.1016/0020-711x(86)90148-5

Cited by 5 publications

(3 citation statements)

References 14 publications

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“…The possibility has been raised that the high salt extraction procedure used for nuclear matrix preparations induces the precipitation of some nuclear proteins ( Kirov and Tsanev, 1986 ). To verify the observations described above with a method that avoids high salt conditions, we used the procedure of Mirkovich et al (1984).…”

Section: Resultsmentioning

confidence: 99%

Components of the Human SWI/SNF Complex Are Enriched in Active Chromatin and Are Associated with the Nuclear Matrix

Reyes

Muchardt

Yaniv

1997

The Journal of Cell Biology

213

182

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Biochemical and genetic evidence suggest that the SWI/SNF complex is involved in the remodeling of chromatin during gene activation. We have used antibodies specific against three human subunits of this complex to study its subnuclear localization, as well as its potential association with active chromatin and the nuclear skeleton. Immunofluorescence studies revealed a punctate nuclear labeling pattern that was excluded from the nucleoli and from regions of condensed chromatin. Dual labeling failed to reveal significant colocalization of BRG1 or hBRM proteins with RNA polymerase II or with nuclear speckles involved in splicing. Chromatin fractionation experiments showed that both soluble and insoluble active chromatin are enriched in the hSWI/SNF proteins as compared with bulk chromatin. hSWI/SNF proteins were also found to be associated with the nuclear matrix or nuclear scaffold, suggesting that a fraction of the hSWI/SNF complex could be involved in the chromatin organization properties associated with matrix attachment regions.

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Section: Resultsmentioning

confidence: 99%

Components of the Human SWI/SNF Complex Are Enriched in Active Chromatin and Are Associated with the Nuclear Matrix

Reyes

Muchardt

Yaniv

1997

The Journal of Cell Biology

213

182

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“…Similarly, Robinson et al (1982) found enrichment of an ovalbumin gene sequence in the DNA associated with the nuclear matrix of oviduct cells. On the other hand, Kirov & Tsanev (1986) and Basler et al (1981) have found essentially opposite results. There are also conflicting results with regard to DNA replication (Djondjurov et al, 1986).…”

Section: Introductionmentioning

confidence: 90%

Preferential association of a transcriptionally active gene with the nuclear matrix of rat fibroblasts transformed by a simian-virus-40–pBR322 recombinant plasmid

Ogata

1990

Biochemical Journal

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To study the relationship between the structural organization and function of the eukaryotic genome, DNA associated with nuclear matrix was analysed by using a transformed rat fibroblast cell line. The nuclear matrices were prepared from the isolated nuclei of pSV1-FR, a rat fibroblast cell line transformed by a pBR322-based recombinant plasmid containing an early gene region, which codes for large T-antigen, of simian virus 40. This transformed cell contained a single copy of the plasmid sequence integrated into the chromosomal DNA of the host cell. The early gene of this plasmid was constitutively expressed, as demonstrated by positive immunofluorescence staining of the cell for large T-antigen and by RNA-blot analysis for its specific mRNA. DNAs were extracted from whole isolated nuclei and nuclear-matrix preparations of the cells, and the relative amounts of the sequence similar to that of the plasmid were compared between these DNA preparations. By employing dot hybridization and Southern-blot analyses we found that the plasmid sequence was more enriched in the DNA extracted from the nuclear matrices than in the DNA extracted from the whole nuclei. When an albumin gene sequence that was not transcribed in this cell line was compared similarly as a control, we found no significant enrichment of this sequence in the DNA associated with the nuclear matrix. Our results strongly support the concept that a transcriptionally active gene is preferentially associated with the nuclear matrix.

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“…The postulated properties of the nuclear matrix imply that it is both a regular structure formed by the self-assembly of one or more unique structural proteins but that it is composed mostly of nucleic acid-binding proteins. Only occasionally has attention has been paid to the solubility characteristics of the abundant nonchromatin proteins, or to the potential for protein aggregation and rearrangement during nuclear isolation, RNA removal, and exposure to salt at Ͼ150 mM and to detergents (Kaufmann and Shaper, 1984;Kaufmann et al, 1986;Mirkovitch et al, 1984;Small et al, 1985;Kirov and Tsanev, 1986). In this paper we report that the conditions typically used to generate the nuclear matrix induce specific hnRNP rearrangements leading to the formation of salt-insoluble filaments that ultrastructurally resemble the filaments observed in nuclear matrix preparations.…”

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confidence: 99%

Nuclear Matrix-like Filaments and Fibrogranular Complexes Form through the Rearrangement of Specific Nuclear Ribonucleoproteins

Tan

Wooley

LeStourgeon

2000

MBoC

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The behavior of nuclear pre-mRNA-binding proteins after their nuclease and/or salt-induced release from RNA was investigated. After RNase digestion or salt extraction, two proteins that initially exist as tetramers (A2) 3 B1 in isolated heterogeneous nuclear ribonucleoprotein (hnRNP) complexes quantitatively reassociated to form regular helical filaments ranging in length from 100 nm to Ͼ10 m. In highly magnified preparations prepared for scanning transmission electron microscopy, single filaments have diameters near 18 nm. In conventional negatively stained preparations viewed at low magnification, the diameters of the thinnest filaments range from 7 to 10 nm. At protein concentrations of Ͼ0.1 mg/ml, the filaments rapidly aggregated to form thicker filamentous networks that look like the fibrogranular structures termed the "nuclear matrix." Like the residual material seen in nuclear matrix preparations, the hnRNP filaments were insoluble in 2 M NaCl. Filament formation is associated with, and may be dependent on, disulfide bridge formation between the hnRNP proteins. The reducing agent 2-mercaptoethanol significantly attenuates filament assembly, and the residual material that forms is ultrastructurally distinct from the 7-to 10-nm fibers. In addition to the protein rearrangement leading to filament formation, nearly one-third of the protein present in chromatin-clarified nuclear extracts was converted to salt-insoluble material within 1 min of digestion with RNase. These observations are consistent with the possibility that the residual material termed the nuclear matrix may be enriched in, if not formed by, denatured proteins that function in pre-mRNA packaging, processing, and transport. INTRODUCTIONWhen nuclei are extensively digested with DNase and RNase and extracted with high-salt solutions, an insoluble residue remains that retains the gross architecture of the nucleus (reviewed by Pederson, 1998Pederson, , 2000. The residue, termed the "nuclear matrix," represents a small percentage of the total nuclear protein mass, but it is very heterogeneous in protein composition (Hodge et al., 1977;Staufenbiel and Deppert, 1983;Kuzmina et al., 1984). The major proteins present in the residue are the nuclear lamins, proteins that constitute elements of the metaphase chromosome and interphase nuclear scaffold, nuclear envelope and pore complex proteins, and numerous proteins associated with heterogeneous nuclear ribonucleoprotein (hnRNP) complexes (as discussed and referenced by Pederson, 1998).Among the numerous other proteins present in the residual material are those that have been hypothesized to form a fibrous network or fibrogranular complex (Berezney and Coffey, 1977;Kaufmann et al., 1981;Gallinaro et al., 1983). On the basis of various experimental observations it has been suggested that the matrix functions in interphase nuclei to bind DNA and organize chromatin (Basler et al., 1981;Brasch and Peters, 1985;Nickerson et al., 1997), that actively transcribing genes and nascent transcripts are associated with...

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Activated murine α-globin gene is not preferentially associated with the nuclear matrix

Cited by 5 publications

References 14 publications

Components of the Human SWI/SNF Complex Are Enriched in Active Chromatin and Are Associated with the Nuclear Matrix

Components of the Human SWI/SNF Complex Are Enriched in Active Chromatin and Are Associated with the Nuclear Matrix

Preferential association of a transcriptionally active gene with the nuclear matrix of rat fibroblasts transformed by a simian-virus-40–pBR322 recombinant plasmid

Nuclear Matrix-like Filaments and Fibrogranular Complexes Form through the Rearrangement of Specific Nuclear Ribonucleoproteins

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