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Karyopherin-me diated import of integral inner nuclear membrane proteins: Nature, Vol. 442, No. 7106. (23 August 2006), pp. 1003-1007.Mega n King, Patrick Lusk, Günter Blobel

Source: Nature, Vol. 442, No. 7106. (23 August 2006), pp. 1003-1007.
The Meaning of Gene Positioning: Cell, Vol. 135, No. 1. (03 October 2008), pp. 9-13.There is no doubt that genomes are organized nonrandomly in the nucleus of higher eukaryotes. But what is the functional relevance of this nonrandomness? In this Essay, we explore the biological meaning of spatial gene positioning by examining the functional link between the activity of a gene and its radial position in the nucleus.T Takizawa, K Meaburn, T Misteli

Source: Cell, Vol. 135, No. 1. (03 October 2008), pp. 9-13.
Phasic dopamine release evoked by abused substances requires cannabinoid receptor activation.: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 27, No. 4. (24 January 2007), pp. 791-795.Transi ent surges of dopamine in the nucleus accumbens are associated with drug seeking. Using a voltammetric sensor with high temporal and spatial resolution, we demonstrate differences in the temporal profile of dopamine concentration transients caused by acute doses of nicotine, ethanol, and cocaine in the nucleus accumbens shell of freely moving rats. Despite differential release dynamics, all drug effects are uniformly inhibited by administration of rimonabant, a cannabinoid receptor (CB1) antagonist, suggesting that an increase in endocannabinoi d tone facilitates the effects of commonly abused drugs on subsecond dopamine release. These time-resolved chemical measurements provide unique insight into the neurobiologica l effectiveness of rimonabant in treating addictive disorders.JF Cheer, KM Wassum, LA Sombers, ML Heien, JL Ariansen, BJ Aragona, PE Phillips, RM Wightman

Source: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 27, No. 4. (24 January 2007), pp. 791-795.
Nuclear inositol lipid metabolism: more than just second messenger generation?: J Cell Biochem, Vol. 96, No. 2. (1 October 2005), pp. 285-292.A distinct polyphosphoino sitide cycle is present in the nucleus, and growing evidence suggests its importance in DNA replication, gene transcription, and apoptosis. Even though it was initially thought that nuclear inositol lipids would function as a source for second messengers, recent findings strongly indicate that lipids present in the nucleus also fulfil other roles. The scope of this review is to highlight the most intriguing advances made in the field over the last few years, such as the possibility that nuclear phosphatidylin ositol (4,5) bisphosphate is involved in maintaining chromatin in a transcriptiona lly active conformation, the new emerging roles for intranuclear phosphatidylin ositol (3,4,5) trisphosphate and phosphoinositi de 3-kinase, and the evidence which suggests a tight relationship between a decreased level of nuclear phosphoinositi de specific phospholipase C-beta1 and the evolution of myelodisplasti c syndrome into acute myeloid leukemia.AM Martelli, MY Follo, C Evangelisti, F Falŕ, R Fiume, AM Billi, L Cocco

Source: J Cell Biochem, Vol. 96, No. 2. (1 October 2005), pp. 285-292.
The nonchromatin substructures of the nucleus: the ribonucleoprot ein (RNP)-containi ng and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy.: J Cell Biol, Vol. 102, No. 5. (May 1986), pp. 1654-1665.The nonchromatin structure or matrix of the nucleus has been studied using an improved fractionation in concert with resinless section electron microscopy. The resinless sections show the nucleus of the intact cell to be filled with a dense network or lattice composed of soluble proteins and chromatin in addition to the structural nuclear constituents. In the first fractionation step, soluble proteins are removed by extraction with Triton X-100, and the dense nuclear lattice largely disappears. Chromatin and nonchromatin nuclear fibers are now sharply imaged. Nuclear constituents are further separated into three well-defined, distinct protein fractions. Chromatin proteins are those that require intact DNA for their association with the nucleus and are released by 0.25 M ammonium sulfate after internucleosom al DNA is cut with DNAase I. The resulting structure retains most heterogeneous nuclear ribonucleoprot ein (hnRNP) and is designated the RNP-containing nuclear matrix. The proteins of hnRNP are those associated with the nucleus only if RNA is intact. These are released when nuclear RNA is briefly digested with RNAase A. Ribonuclease digestion releases 97% of the hnRNA and its associated proteins. These proteins correspond to the hnRNP described by Pederson (Pederson, T., 1974, J. Mol. Biol., 83:163-184) and are distinct from the proteins that remain in the ribonucleoprot ein (RNP)-depleted nuclear matrix. The RNP-depleted nuclear matrix is a core structure that retains lamins A and C, the intermediate filaments, and a unique set of nuclear matrix proteins (Fey, E. G., K. M. Wan, and S. Penman, 1984, J. Cell Biol. 98:1973-1984). This core had been previously designated the nuclear matrix-interme diate filament scaffold and its proteins are a third, distinct, and nonoverlapping subset of the nuclear nonhistone proteins. Visualizing the nuclear matrix using resinless sections shows that nuclear RNA plays an important role in matrix organization. Conventional Epon-embedded electron microscopy sections show comparatively little of the RNP-containing and RNP-depleted nuclear matrix structure. In contrast, resinless sections show matrix interior to be a three-dimensio nal network of thick filaments bounded by the nuclear lamina. The filaments are covered with 20-30-nm electron dense particles which may contain the hnRNA. The large electron dense bodies, enmeshed in the interior matrix fibers, have the characteristic morphology of nucleoli. Treatment of the nuclear matrix with RNAase results in the aggregation of the interior fibers and the extensive loss of the 20-30-nm particles.(ABS TRACT TRUNCATED AT 400 WORDS)EG Fey, G Krochmalnic, S Penman

Source: J Cell Biol, Vol. 102, No. 5. (May 1986), pp. 1654-1665.
Tightly bound somatic histones in mature ram sperm nuclei.: FEBS Lett, Vol. 138, No. 1. (8 February 1982), pp. 50-54.A Uschewa, Z Avramova, R Tsanev

Source: FEBS Lett, Vol. 138, No. 1. (8 February 1982), pp. 50-54.
Chromosome territories, interchromatin domain compartment, and nuclear matrix: an integrated view of the functional nuclear architecture.: Crit Rev Eukaryot Gene Expr, Vol. 10, No. 2. (2000), pp. 179-212.Advanc es in the specific fluorescent labeling of chromatin in fixed and living human cells in combination with three-dimensio nal (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 suprachromosom al 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-replicat ing 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 compartmentali zed nuclear architecture and its functional consequences.T Cremer, G Kreth, H Koester, RH Fink, R Heintzmann, M Cremer, I Solovei, D Zink, C Cremer

Source: Crit Rev Eukaryot Gene Expr, Vol. 10, No. 2. (2000), pp. 179-212.
Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation: FASEB J., Vol. 15, No. 7. (1 May 2001), pp. 1236-1238.10.1 096/fj.00-0655 fjeHenning Pfeifer, Marcus Conrad, Doris Roethlein, Antonios Kyriakopoulos, Markus Brielmeier, Georg Bornkamm, Dietrich Behne

Source: FASEB J., Vol. 15, No. 7. (1 May 2001), pp. 1236-1238.
The principles of nuclear structure.: Chromosome Res, Vol. 11, No. 5. (2003), pp. 387-401.In multicellular eukaryotes, chromatin function is regulated by numerous extremely sophisticated mechanisms. Recent developments in our ability to monitor the organization and dynamic properties of the components involved in processes such as gene expression and DNA synthesis have emphasised how both global nuclear architecture and chromosome structure can influence these fundamental processes. This review sets out to evaluate our present views of the principles that dictate nuclear structure. Particular emphasis is placed on architectural themes and the concept of spatial epigenetics.DA Jackson

Source: Chromosome Res, Vol. 11, No. 5. (2003), pp. 387-401.
In situ detection of a DNA-polymerase activity in the nuclei of mouse spermatozoa.: Chromosoma, Vol. 54, No. 1. (27 January 1976), pp. 33-37.A nuclear DNA-polymerase activity has been detected in situ in mouse spermatozoa with a cytochemical method. The acid-insoluble radioactive product obtained after incubation in a mixture containing all four deoxyribonucle oside 5'-triphosphat es, Mg++,KCl and dithiothreitol (DTT) was completely removed by DNAse but was insensitive to RNAse and pronase action. The polymerization reaction did not take place in the presence of only one nucleotide and was dramatically reduced when actinomycin D was present; it did not seem to be inhibited markedly by N-ethylmaleimi de (NEM) or by parahydroxymer curibenzoate (PHMB) but was sensitive to high concentrations of KCl.--The reaction depended strictly on the presence of nuclear DNA as template since treatment with pancreatic DNAae before the DNA-polymerase assay completely prevented the appearance of any radioactivity. P Chevaillier, M Philippe

Source: Chromosoma, Vol. 54, No. 1. (27 January 1976), pp. 33-37.

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