The Nuclear Matrix: A Structural Milieu for the Intranuclear Attachment and Replication of Eucaryotic DNA

Berezney, Ronald

doi:10.1007/978-3-662-39932-3_26

Cited by 3 publications

(4 citation statements)

References 45 publications

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“…A variety of methods are now available for permeabilizing cells (Bell, 1981) or preparing selectively extracted nuclear preparations (Berezney, 1981). For such material, soluble components are washed out during the preparative treatment.…”

Section: Discussionmentioning

confidence: 99%

Freeze fracture through the cytoskeleton, nucleus and nuclear matrix of lymphocytes studied by scanning electron microscopy

Haggis

Schweitzer

Hall

et al. 1983

Journal of Microscopy

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SUMMARY The technique of delaying fixation until after freeze‐fracture and thawing, described in an earlier paper (Haggis & Bond, 1979), has been developed further for study of cells in culture, principally mouse lymphocytes stimulated by concanavalin A. Using a thin layer of cells, a cryoprotectant concentration of either 10% glycerol or dimethylsulphoxide, is sufficient to give good structural preservation after rapid freezing and thawing. Nuclear matrices and Triton‐permeabilized cells have been prepared from stimulated lymphocytes for comparative study. Polylysine‐coated fibrin support films have been found to provide a convenient means of handling cells and subcellular preparations during freeze fracture, critical point drying and mounting for high‐resolution scanning electron microscopy.

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Section: Discussionmentioning

confidence: 99%

Freeze fracture through the cytoskeleton, nucleus and nuclear matrix of lymphocytes studied by scanning electron microscopy

Haggis

Schweitzer

Hall

et al. 1983

Journal of Microscopy

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“…Nuclear matrix has been described as the insoluble, skeletal framework of the nucleus. Many other functional properties have been found associated with the nuclear matrix including DNA loop attachment sites (Dijkwel et Berezeny & Buchholtz, 1981a; Razin et al, 1981), in vivo replicating DNA (Vogelstein et al, 1980: Berezney & Buchholtz, 1981b), DNA polymerase a (Smith & Berezney, 1980), DNA synthesis (Berezney & Smith, 1981; Smith & Berezney, 1982); and the avian oviduct ovalbumin and other transcriptionally active genes (Robinson et al, 1982;Ciejek et al, 1983). This and other laboratories have previously reported that the nuclear acceptor sites for the avian oviduct progesterone receptor (PR)1 *consist both of genomic DNA and of specific chromatin proteins termed acceptor proteins (O'Malley et al, 1972;Webster et al, 1976;Hora et al, 1986;Spelsberg et al, 1971Spelsberg et al, , 1972Spelsberg et al, , 1983Spelsberg et al, , 1988Spelsberg et al, , 1989. Similar compositions for the nuclear acceptor sites of a variety of steroid target tissue •This research was supported in part by NIH Grant HD9140 and by the Mayo Foundation.…”

mentioning

confidence: 99%

Nuclear matrix localization and specific matrix DNA binding by receptor binding factor 1 of the avian oviduct progesterone receptor

et al. 1991

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A chromatin acceptor protein for the avian oviduct progesterone receptor (PR), termed receptor binding factor 1 (RBF-1), has recently been shown to (1) be a component of the nuclear binding sites (acceptor sites) for PR and (2) generate high-affinity binding sites (termed the RBF-1 class of sites) on avian genomic DNA [Schuchard et al. (1991) Biochemistry 30, 4535-4542]. A second class of sites and its associated protein (termed RBF-2) were also identified. This paper demonstrates that RBF-1 and also the PR nuclear binding sites are localized in the oviduct nuclear matrix. RBF-1 is found in abundance in the nuclear matrix of liver but only in traces in the nuclear matrix of spleen. Extraction of the nuclear matrix with 4.0 M Gdn-HCl results in the complete removal of RBF-1 as occurs with whole chromatin. Interestingly, a second class of specific PR binding, termed RBF-2, remains on the nuclear matrix after the removal of all RBF-1. Southern blot analysis indicates that the nuclear matrix DNA contains sequences homologous with the 5'-flanking domains of the rapidly steroid regulated c-myc and c-jun protooncogenes and the beta-actin gene, but not genomic sequences of the late sex steroid regulated gene, ovalbumin, or the alpha-actin gene. A specific, small region in the 5'-flanking domain of the c-myc gene appears to be associated with the nuclear matrix. Southwestern blot analysis using partially purified RBF-1 shows a marked affinity and specificity of the RBF-1 for the nuclear matrix DNA.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The proteins of the nuclear matrix (Berezney and Coffey, 1974) are capable of very tight binding to DNA and are also involved in the processes of transcription and replication (review, Berezney, 1981). Because of these two properties it is reasonable to suggest that the association between the nuclear matrix proteins and DNA may alter during DNA replication.…”

Section: N6a 5b7mentioning

confidence: 99%

“…1A) are seen to possess isoelectric points of approximately 6.5 to 7. Proteins 6 and 7 were identified as variants of lamin a, one of the major nuclear matrix proteins that constitutes the envelope surrounding the nucleus (Berezney, 1981), by their abundance in the nuclear matrix fraction, molecular weights, and iso- electric point. These criteria have been used previously for the identification of lamina protein (Laliberte et al, 1984;Kaufmann et al, 1983;Shelton et al, 1980;Lebel and Raymond, 1984;Dagenais et al, 1984;Kaufmann and Shaper, 1984).…”

Section: Identification Of Nuclear Matrix Proteins From Swiss 3t3 Cellsmentioning

confidence: 99%

Synthesis and stability of nuclear matrix proteins in resting and serum‐stimulated swiss 3T3 cells

Milavetz

Edwards

1986

Journal Cellular Physiology

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The major [35S]methionine-radiolabeled nuclear matrix proteins of mouse 3T3 cells were isolated, and most of these were found to be similar in molecular weight, charge, and protease fingerprint to the nuclear matrix proteins of African green monkey kidney cells, which are found tightly bound to simian virus 40 chromosomes. These nuclear matrix proteins were found to be synthesized in quiescent and serum-stimulated cells and to be turned over slowly during pulse-chase experiments. In contrast, a 70-Kd (kilodalton) neutral protein identified as lamin a was found to be turned over rapidly, producing a 68-Kd protein with a similar isoelectric point. In addition, we observed a decrease in the amounts of two chromatin-bound matrix proteins and a relative increase in lamin a following labeling in the presence of 2 micrograms/ml actinomycin D. However, these effects do not appear to be a result of inhibition of transcription, since they were not observed with other inhibitors (alpha-amanitin and 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole).

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The Nuclear Matrix: A Structural Milieu for the Intranuclear Attachment and Replication of Eucaryotic DNA

Cited by 3 publications

References 45 publications

Freeze fracture through the cytoskeleton, nucleus and nuclear matrix of lymphocytes studied by scanning electron microscopy

Freeze fracture through the cytoskeleton, nucleus and nuclear matrix of lymphocytes studied by scanning electron microscopy

Nuclear matrix localization and specific matrix DNA binding by receptor binding factor 1 of the avian oviduct progesterone receptor

Synthesis and stability of nuclear matrix proteins in resting and serum‐stimulated swiss 3T3 cells

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