Übersicht über die Turbinen

Adolph, Max

doi:10.1007/978-3-642-88294-4_11

Cited by 3 publications

(3 citation statements)

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“…In addition, there are other nuclear proteins, with similar molecular weights. Tncluded are those of the nuclear envelope [20-231, nuclear matrix [7] and scaffold [24], or the nuclear contractile proteins [10,25]. Their Phoretic Patterns [7,10, revealed little Similarity to S1 Proteins.…”

Section: (-)mentioning

confidence: 99%

A set of non‐histone proteins isolated from the nuclei of various rat tissues

Inoue

Higashi

Hasuma

et al. 1983

European Journal of Biochemistry

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A set of non-histone proteins has been identified in the nuclei from liver, brain, spleen and testis tissues of the rat. Following moderate digestion of thoroughly washed nuclei with DNase 1 or micrococcal nuclease, EDTA was added to 5 m M to the reaction mixture and the preparation centrifuged. We found that the supernatant contained a limited amount of non-histone proteins (fraction SI). Sodium dodecyl sulfate (SDS) gel electrophoresis revealed S1 to be composed of a remarkably simple set of proteins resolved into four groups (A -D) each possessing closely spaced doublets or a triplet. Their molecular weights were A, 76100-80000; B, 48200-49500; C, 44500-45200 and D, 39500-41 500. The yield suggested that these proteins were structural constituents; however, they did not coincide with the known structural proteins of the cell nucleus. Two-dimensional gel electrophoresis further resolved each of the SDS bands into as many as nine spots, according to various charges. Some were labelled with [32P]orthophosphate in vivo, or with [y-32P]ATP and purified nuclear protein kinase NII in vitro. The released proteins B -D had fairly constant relative molar ratios at various times of digestion, thereby indicating possible localizations a t similar sites in the nucleus. The kinetic data together with the aggregation property at neutral pH values and the solubility in 5 mM EDTA suggest that proteins B -D constitute a group of proteins that have several common characteristics.The abundance of protein species in the cell nucleus varies with the protein; some are structural or regulatory in function while others are catalytic in various biochemical processes. Isolation and characterization of these nuclear proteins should greatly aid in understanding the structure and function of the nucleus as well as the molecular properties of the protein in question. Isolation of a group of proteins which share molecular properties may be advantageous, as a common biological function may be involved. The precedent of this can be illustrated with histones and high mobility group (HMG) proteins. Histones, the building molecules of the nucleosomes [I], can be readily extracted in a set from the chromatin with dilute mineral acids [2]; H M G proteins, which confer a structural characteristic of the active Chromatin [3], are extracted as a group from chromatin with 0.35 M NaCl and remain soluble in 2There have been numerous studies on various nuclear architectures such as chromatin, nuclear matrix and nuclear envelopes. One approach is to use DNA-hydrolyzing enzymes ; for example, DNase I has been used to distinguish the transcriptionally active from the bulk chromatin in differential digestion kinetics [5], or to isolate the nuclear pore complexlamina fraction [6] and nuclear matrix [7].In our studies on nuclear proteins we were interested in protein components liberated from the nuclei by digestion with DNA-hydrolyzing enzymes. We report here that a novel and remarkably simple set of non-histone proteins was isolated from the nuclei by nucle...

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Section: (-)mentioning

confidence: 99%

A set of non‐histone proteins isolated from the nuclei of various rat tissues

Inoue

Higashi

Hasuma

et al. 1983

European Journal of Biochemistry

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“…Numerous studies have Indicated that the eucaryotic genome Is organized Into a series of supercolled loops which are anchored to a nuclear skeleton or matrix (reviewed In 1). Although the composition of the nuclear matrix is a subject of controversy (2,3), several lines of evidence, Including biophysical, morphological and biochemical experiments, support the Idea that the genome Itself Is topologically constrained In the form of loops by a skeletal structure (4)(5)(6)(7)(8)(9).…”

Section: Ntroulct Ionmentioning

confidence: 99%

The anatomy of supercoiled loops in theDrosophila, 7F locus

Small

Vogelstein

1985

Nucl Acids Res

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The genome in eucaryotes is organized into a series of supercoiled loops, topologically anchored at their bases by components of the nuclear matrix. Previous studies have shown that active genes are associated with the nuclear matrix. We wished to know whether loops in general were solely organized by active genes. We therefore examined a locus of the Drosophila X-chromosome comprising 163,000 bp of continuous DNA sequences and devoid of known active genes. Of the 52 EcoRI restriction fragments comprising this region, we found 5 anchored fragments which non-randomly organized this region into 4 DNA loops. Each of the 5 anchored fragments contained a transcribed sequence. These results strongly suggest that supercoiled loops are organized in a specific fashion with respect to DNA sequence, with the anchorage points exclusively demarcated by transcriptionally active genes.

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“…This substructure has been termed the nuclear matrix (Berezney & Coffey, 1974), the nuclear scaffold (Adolph, 1980), the nuclear cage (Cook & Brazell, 1980), or the interphase genome skeleton (Hancock, 1982). In addition to the maintenance of the three-dimensional structure of the nucleus, evidence for a more dynamic role for a nuclear matrix has been presented; e.g., DNA replication appears to take place in association with a nuclear matrix (Berezney & Buchholtz, 1981b;Pardoll et al, 1980), and DNA polymerase has been found tightly associated with nuclear matrix preparations (Smith & Berezney, 1980).…”

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confidence: 99%

Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction

Olson¹,

Wallace²,

Herrera³

et al. 1986

Biochemistry

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Biochemical and morphological studies were performed on Novikoff hepatoma ascites cell nucleolar matrix fractions prepared by deoxyribonuclease I digestion and high-molarity salt extractions essentially according to a published method [Berezney, R., & Buchholz, L. A. (1981) Exp. Cell Res. 20, 4995-5002]. The nucleolar matrix fraction was enriched in polypeptides of molecular mass of 28, 37.5, 40, 70, 72, 110 (protein C23), and 160 kDa, compared to the nuclear fraction in which polypeptides of molecular mass of 31, 33.5, 43.5, 46, 50, 56, and 59 kDa were predominant. About one-fourth of the protein, half of the RNA, and less than 4% of the DNA originally present in the nucleoli remained in the matrix fraction. Addition of single agents such as ethylenediaminetetraacetic acid, ribonuclease A, or mercaptoethanol during preparation had no significant effect on the polypeptide composition of the nucleolar matrix fraction. However, the combination of mercaptoethanol and ribonuclease A caused most of the RNA and protein to be removed, including protein C23 and the 160-kDa polypeptide, with polypeptides in the range of Mr 30 000-50 000 remaining. Electron microscopy of nucleolar matrix fractions revealed the presence of particles similar in size to the granular elements of nucleoli. However, when ribonuclease A and mercaptoethanol were included in the procedure, only amorphous material remained. Many proteins of nucleolar preribosomal RNP particles were also associated with the nucleolar matrix fraction. RNA from the nucleolar matrix fraction was enriched in sequences from 18S and 28S ribosomal RNA. These results indicate that preribosomal RNP particles are major constituents of a nucleolar matrix fraction prepared by the deoxyribonuclease I-high-molarity salt method.

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Übersicht über die Turbinen

Cited by 3 publications

References 0 publications

A set of non‐histone proteins isolated from the nuclei of various rat tissues

A set of non‐histone proteins isolated from the nuclei of various rat tissues

The anatomy of supercoiled loops in theDrosophila, 7F locus

Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction

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