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COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast.

The cytosolic yeast proteins Sec13p-Sec31p, Sec23p-Sec24p, and the small GTP-binding protein Sar1p generate protein transport vesicles by forming the membrane coat termed COPII. We demonstrate by thin section and immunoelectron microscopy that purified COPII components form transport vesicles directly from the outer membrane of isolated yeast nuclei. Another set of yeast cytosolic proteins, coatomer and Arf1p (COPI), also form coated buds and vesicles from the nuclear envelope. Formation of COPI-coated, but not COPII-coated, buds and vesicles on the nuclear envelope is inhibited by the fungal metabolite brefeldin A. The two vesicle populations are distinct. However, both vesicle types are devoid of endoplasmic reticulum (ER) resident proteins, and each contains targeting proteins necessary for docking at the Golgi complex. Our data suggest that COPI and COPII mediate separate vesicular transport pathways from the ER.

Anti-Bacterial Agents↗

Two-color green fluorescent protein time-lapse imaging.

The Aequorea victoria green fluorescent protein (GFP) is widely recognized as a powerful tool in cell biology, serving as a vital reporter for monitoring localization and dynamics of intracellular proteins and organelles over time. GFP variants with shifted spectral characteristics have been described and offer enormous potential for double-labeling experiments and protein-protein interaction studies. However, most GFP variant combinations are not suitable for double-label, time-lapse imaging experiments because of either extremely rapid photobleaching of blue-shifted GFP variants or crossover of their excitation and emission spectra, which must then be computer corrected. Here, we describe the successful use of two photostable spectral GFP variants, W7 and 10C, in dual-color, time-lapse imaging of fusion proteins in living cells using either wide-field or confocal microscopy. W7 and 10C were highly photostable during repetitive long-term imaging and were cleanly separated by their different excitation spectra alone with negligible crossover of fluorescence. We present time-lapse image sequences of COS-7 cells co-expressing both a marker of the Golgi complex (galactosyl transferase) fused to W7 and a marker of the nuclear envelope (lamin-B receptor) fused to 10C. To our knowledge, these image sequences provide the first simultaneous visualization of Golgi and nuclear envelope membranes in living cells.

Animals↗

THE ULTRASTRUCTURE OF A MAMMALIAN CELL DURING THE MITOTIC CYCLE.

With a technique of preselecting the mitotic cell in the living state for subsequent electron microscopy, it has been possible to examine the ultrastructure of the various stages of mitosis with greater precision than has been reported previously. The early dissolution of the nuclear envelope has been found to be preceded by a marked undulation of this structure within the nuclear "hof." This undulation appears to be intimately related to the spindle-forming activity of the centriole at this time. Marked pericentriolar osmiophilia and extensive arrays of vesicles are also prominent at this stage, the former continuing into anaphase. Progression of the cell through prophase is accompanied by a disappearance of these vesicles. A complex that first makes its appearance in prophase but becomes most prominent in metaphase is a partially membrane-bounded cluster of dense osmiophilic bodies. These clusters which have a circumferential distribution in the mitotic cell are shown to be derived from multivesicular bodies and are acid phosphatase-positive. The precise selection of cells during the various stages of anaphase has made it possible to follow chronologically the morphological features of the initiation of nuclear membrane reformation. The nuclear membrane appears to be derived from polar aggregates of endoplasmic reticulum, and the process begins less than 2 minutes after the onset of karyokinesis. While formation of the nuclear envelope is initiated on the polar aspects of the chromatin mass, envelope elements appear on the equatorial aspect long before the polar elements fuse. Apparently interfering with this fusion are continuous spindle tubules which traverse the chromatin mass in striking density at characteristic points. Several cortical changes, also most pronounced in anaphase, have been described, as has the kinetochore which is seen to good advantage only in this stage. The Golgi complex has been found to disappear both morphologically and histochemically during mitosis and to reappear rapidly in telophase. Evidence is presented which implicates the continuous spindle tubules in certain phases of chromosome movement.

Anaphase↗

Chloroplast development in Ochromonas danica.

When dark-grown cells of Ochromonas danica are placed in the light, the amount of chlorophyll a per cell increases 82-fold; the content of carotenoid pigment, 24-fold. Concomitantly with this increase in chlorophyll and carotenoid pigment, the small proplastid of dark-grown cells develops into a large lamellate chloroplast. During the first 12 hours in the light, vesicles appear within the loose clusters of dense chloroplast granules, enlarge, align themselves into rows (plates in three dimensions), and fuse into discs. Double discs may form from the more or less simultaneous fusion of two adjacent plates of vesicles or by the addition of vesicles to an already formed single disc. Three-disc bands arise by the addition of a disc to an already formed two-disc band through the approach and fusion of more vesicles. After 24 hours in the light, most of the chloroplast bands contain three discs, but the chloroplasts are still small. After 48 hours in the light, almost all the cells contain full-sized chloroplasts with a full complement of three-disc bands. However, at this time the amount of chlorophyll a and carotenoid pigment is only one-half of maximum. During the next 3 days in the light, as the number of chlorophyll and carotenoid molecules per chloroplast approximately doubles, there is a compression of the discs in each band (from 180 to 130 A) and a precise alignment of their membranes. Changes also occur in the nucleus when dark-grown cells are placed in the light. There is an increase in the number of small nucleolar bodies, many of which lie directly against the nuclear envelope, and in a few cells a dense mass of granules is seen between the two membranes of the nuclear envelope.

Carotenoids↗

Local InsP3-dependent perinuclear Ca2+ signaling in cardiac myocyte excitation-transcription coupling.

Previous work showed that calmodulin (CaM) and Ca2+-CaM-dependent protein kinase II (CaMKII) are somehow involved in cardiac hypertrophic signaling, that inositol 1,4,5-trisphosphate receptors (InsP3Rs) in ventricular myocytes are mainly in the nuclear envelope, where they associate with CaMKII, and that class II histone deacetylases (e.g., HDAC5) suppress hypertrophic gene transcription. Furthermore, HDAC phosphorylation in response to neurohumoral stimuli that induce hypertrophy, such as endothelin-1 (ET-1), activates HDAC nuclear export, thereby regulating cardiac myocyte transcription. Here we demonstrate a detailed mechanistic convergence of these 3 issues in adult ventricular myocytes. We show that ET-1, which activates plasmalemmal G protein-coupled receptors and InsP3 production, elicits local nuclear envelope Ca2+ release via InsP3R. This local Ca2+ release activates nuclear CaMKII, which triggers HDAC5 phosphorylation and nuclear export (derepressing transcription). Remarkably, this Ca2+-dependent pathway cannot be activated by the global Ca2+ transients that cause contraction at each heartbeat. This novel local Ca2+ signaling in excitation-transcription coupling is analogous to but separate (and insulated) from that involved in excitation-contraction coupling. Thus, myocytes can distinguish simultaneous local and global Ca2+ signals involved in contractile activation from those targeting gene expression.

Active Transport, Cell Nucleus↗

Changes of free calcium levels with stages of the cell division cycle.

Although the regulation of events in the cell division cycle by calcium or other cations has been the subject of much interest and speculation, experimental studies have been hampered by the difficulty of measuring submicromolar intracellular free calcium concentrations ([Ca2+]i) over an entire cell cycle. We now describe experiments using a new fluorescent calcium chelator, fura-2 (see Fig. 1c for structure), for continuous measurement of [Ca2+]i from fertilization through the first cleavage of individual eggs of the sea urchin Lytechinus pictus. We also show for comparison the results of parthenogenetic activation by ammonia. In addition to the known transient rise of [Ca2+]i at fertilization, further peaks are now revealed during pronuclear migration, nuclear envelope breakdown, the metaphase/anaphase transition and cleavage. Parthenogenetic activation by ammonia also elicits a sustained rise starting at nuclear envelope breakdown.

Ammonia↗

Inhibition of human cytomegalovirus maturation by brefeldin A.

Brefeldin A (BFA) was found to interfere with specific events of human cytomegalovirus (HCMV) maturation in human fibroblasts. Ultrastructural as well as biochemical studies suggested that short-term exposure of infected cultures to BFA during the late infectious cycle primarily prevented Golgi-dependent processes, e.g. envelopment of naked cytoplasmic nucleocapsids in the trans-Golgi network (TGN) and normal processing of glycoprotein B. In contrast, the nuclear phase of viral morphogenesis, e.g. transport budding at the nuclear envelope, was not impaired. These observations were compatible with the interpretation that HCMV morphogenesis may involve sequential budding events at the nuclear envelope and at cisternae of the TGN. BFA treatment during the early infectious cycle efficiently inhibited HCMV-DNA synthesis and thus late viral functions, preventing production of viral progeny. Cytotoxicity was excluded as a cause for these findings.

Antiviral Agents↗

Anucleate fragments of parthenogenetic eggs and of maturing oocytes contain complementary factors required for development of a male pronucleus.

Eight-h-old anucleate fragments of artificially activated mouse oocytes produced within 30 min after activation were fused with anucleate fragments of ovarian oocytes bisected at the GV stage and matured in vitro for 4-5 h. The resulting cybrids were inseminated soon after fusion and fixed 3-4 h or 14 h later. After 3-4 h of culture most of the sperm nuclei underwent decondensation. Early male pronuclei were observed sporadically. After overnight culture small or fully formed male pronuclei were present in monospermic and dispermic cybrids. The abortive nuclei, designated as stage IIa (earlier described by Borsuk and Tarkowski, 1989) were also observed and their occurrence was strongly correlated with the rate of polyspermy. In unfused (control) anucleate fragments of maturing and activated oocytes inseminated at the same time as the cybrids, male pronuclei were never observed. These results show that the cytoplasms of activated eggs and of maturing oocytes contain complementary factors required for the transformation of the sperm nucleus into the male pronucleus. The former has lost the capability to break down the sperm nucleus envelope but contains factors required for pronuclear growth. The latter is able only to initiate the process of transformation, i.e., to break down the nuclear envelope and decondense the denuded sperm chromatin. However, the activity of the factor responsible for nuclear envelope breakdown is limited because in cybrids penetrated by more than two spermatozoa, transformation of sperm nuclei was usually abnormal.

Animals↗

ARF is not required for nuclear vesicle fusion or mitotic membrane disassembly in vitro: evidence for a non-ARF GTPase in fusion.

Xenopus laevis egg extracts are a well-characterized system for studying nuclear envelope dynamics in vitro. ADP-ribosylation factor (ARF), a 21 kDa GTPase involved in vesicular transport, inhibits nuclear vesicle fusion in vitro when membranes are preincubated with ARF and GTP gamma S (Boman et al., Nature 358, 512-514 (1992)). To test the hypothesis that ARF was required for nuclear envelope assembly or disassembly, we examined these events in cytosol from which ARF was depleted by size fractionation or inhibited with brefeldin A (BFA). In ARF-depleted extracts, vesicles bound chromatin and fused to enclose the chromatin, but the resulting enclosed nuclei lacked pore complexes and remained small. Further growth was not stimulated by adding ARF1, suggesting that fractionation removed other proteins required for pore complex assembly and nuclear growth. Nuclei assembled in ARF-depleted extracts, and rat liver nuclei, disassembled normally in mitotic ARF-depleted reactions. BFA, which inhibits ARF binding to membranes, had no effect on nuclear assembly or disassembly. We concluded that ARF is not essential for nuclear membrane dynamics. Nuclear vesicle fusion was still inhibited by GTP gamma S in ARF-depleted reactions and in reactions containing BFA, strongly suggesting that there is another unidentified GTPase that is either required for vesicle fusion or capable of inhibiting fusion in the presence of GTP gamma S.

ADP-Ribosylation Factor 1↗

The human ALL-1/MLL/HRX antigen is predominantly localized in the nucleus of resting and proliferating peripheral blood mononuclear cells.

The ALL-1 gene is an important regulator of embryonal and hematopoietic development, and structural variants of the human gene generated by chromosomal translocations and other genomic alterations presumably act as oncogenes in the pathogenesis of acute leukemias and other hematological malignancies. Antisera against two different epitopes of the human ALL-1 protein (anti-ALL1-N and anti-ALL1-C) were produced. Both sera revealed indistinguishable patterns of antigen localization in human peripheral blood mononuclear cells (PBMCs). In resting PBMCs, the antigen was distributed in a speckled pattern across the nuclei, with an increased density at the nuclear envelope and the nuclear indentation. In mitotically stimulated PBMCs, the antigen surrounded the condensing chromosomes but did not colocalize with chromatin or the nuclear scaffold. The antigen is considered a marker for a novel nuclear subcompartment, a perichromosomal area termed the "chromosomal envelope." In Western blot experiments, the anti-ALL1-N serum reacted with a polypeptide corresponding to the expected full-length 430-kDa ALL-1 protein. Recombinant proteins representing the AT-hook and zinc binding subdomains of the ALL-1 protein interacted in vitro with a degenerate mixture of double-stranded oligodeoxynucleotides. Thus, the ALL-1 protein probably is a DNA-binding protein with both a sequence-unspecific (AT-hook) and a sequence-specific (zinc binding subdomains) double-stranded DNA binding mode.

Animals↗

Prelamin A farnesylation and progeroid syndromes.

Hutchinson-Gilford progeria syndrome (HGPS) is caused by a LMNA mutation that leads to the synthesis of a mutant prelamin A that is farnesylated but cannot be further processed to mature lamin A. A more severe progeroid disorder, restrictive dermopathy (RD), is caused by the loss of the prelamin A-processing enzyme, ZMPSTE24. The absence of ZMPSTE24 prevents the endoproteolytic processing of farnesyl-prelamin A to mature lamin A and leads to the accumulation of farnesyl-prelamin A. In both HGPS and RD, the farnesyl-prelamin A is targeted to the nuclear envelope, where it interferes with the integrity of the nuclear envelope and causes misshapen cell nuclei. Recent studies have shown that the frequency of misshapen nuclei can be reduced by treating cells with a farnesyltransferase inhibitor (FTI). Also, administering an FTI to mouse models of HGPS and RD ameliorates the phenotypes of progeria. These studies have prompted interest in testing the efficacy of FTIs in children with HGPS.

Animals↗

The mitotic spindle and associated membranes in the closed mitosis of trichomonads.

In the present work, we followed the several phases of Tritrichomonas foetus and Trichomonas vaginalis cell cycles using immunofluorescence, serial thin sections, three-dimensional (3D) reconstruction, and transmission electron microscopy. In motile trichomonad cells or in pseudocyst forms, the nuclear envelope persists throughout mitosis, and the spindle is extranuclear. We found three types of spindle microtubules: pole-to-nucleus microtubules which are attached to the nuclear envelope, pole-to-pole microtubules forming a cylindrical, cytoplasmic groove on the nuclear compartment in pseudocysts of T. foetus cells, and pole-to-cytosol microtubules which extend freely into the cytoplasm. We demonstrated that: (1) in T. foetus, the spindle is assembled from an MTOC located at the base of the costa, underneath one of the basal bodies; (2) the spindle presents an unusual arc shape during the initial phases of mitosis in motile trophozoites; (3) the spindle microtubules are glutamylated, but not acetylated; (4) several membranes similar to those of the endoplasmic reticulum follow the spindle microtubules; (5) finger-like projections extend from the nucleus towards the cell poles in pseudocysts and multinucleated cells; and (6) vesicles formed in between the two nuclear membranes are seen in the course of mitosis in both trophozoite and pseudocyst forms.

Animals↗

DNA replication in cell-free extracts from Drosophila melanogaster.

We have developed an efficient in vitro replication system from 0-2 h Drosophila melanogaster embryos. Demembranated Xenopus sperm DNA when incubated in such an extract first becomes enclosed in a nucleus-like structure with a nuclear envelope and a karyoskeleton. It then undergoes one round of semiconservative replication--this replication appears completely dependent on nuclear formation. Up to 30% of input DNA is nucleated in one reaction. Efficient nuclear formation and replication are dependent on a cold treatment step, prior to disruption of the embryos. They also depend on the age of the embryos used. Extracts from older embryos (0-5 h) are capable of nuclear formation, although at a much reduced efficiency, and repair synthesis, but seem to have lost the ability to initiate DNA replication. In addition to replicating sperm DNA this system appears capable of carrying out semi-conservative replication on some plasmids. However, it cannot use these to trigger nuclear formation; replication is only seen if the plasmids are coincubated with sperm DNA. The in vitro formed nuclei have not been observed to trigger nuclear envelope breakdown and entry into mitosis. However, they can re-replicate the DNA if the nuclei are permeabilized. This system should be a useful complement to the previously isolated Xenopus in vitro replication system. In addition the amenability of Drosophila to genetic study should open up new approaches not previously possible with Xenopus.

Animals↗

Nuclear import of the retrotransposon Tf1 is governed by a nuclear localization signal that possesses a unique requirement for the FXFG nuclear pore factor Nup124p.

Retroviruses, such as human immunodeficiency virus, that infect nondividing cells generate integration precursors that must cross the nuclear envelope to reach the host genome. As a model for retroviruses, we investigated the nuclear entry of Tf1, a long-terminal-repeat-containing retrotransposon of the fission yeast Schizosaccharomyces pombe. Because the nuclear envelope of yeasts remains intact throughout the cell cycle, components of Tf1 must be transported through the envelope before integration can occur. The nuclear localization of the Gag protein of Tf1 is different from that of other proteins tested in that it has a specific requirement for the FXFG nuclear pore factor, Nup124p. Using extensive mutagenesis, we found that Gag contained three nuclear localization signals (NLSs) which, when included individually in a heterologous protein, were sufficient to direct nuclear import. In the context of the intact transposon, mutations in the NLS that mapped to the first 10 amino acid residues of Gag significantly impaired Tf1 retrotransposition and abolished nuclear localization of Gag. Interestingly, this NLS activity in the heterologous protein was specifically dependent upon the presence of Nup124p. Deletion analysis of heterologous proteins revealed the surprising result that the residues in Gag with the NLS activity were independent from the residues that conveyed the requirement for Nup124p. In fact, a fragment of Gag that lacked NLS activity, residues 10 to 30, when fused to a heterologous protein, was sufficient to cause the classical NLS of simian virus 40 to require Nup124p for nuclear import. Within the context of the current understanding of nuclear import, these results represent the novel case of a short amino acid sequence that specifies the need for a particular nuclear pore complex protein.

Active Transport, Cell Nucleus↗

Mechanism of arachidonic acid-induced Ca2+ mobilization in liver nuclei.

Arachidonic acid treatment in isolated liver nuclei resulted in a rapid and transient increase of Ca2+ concentration in the nucleoplasm which was monitored with the Ca(2+)-sensitive dye fura-2 dextran. This effect was associated with a decrease of Ca2+ concentration in the nuclear envelope as measured with fura-2 AM. Our results indicate that arachidonic acid causes a Ca2+ release from the nuclear envelope to the nucleoplasm similar to that evoked by inositol trisphosphate (IP3). The arachidonic acid-induced Ca2+ mobilization in the nucleus was not due to the metabolites of arachidonic acid. Experiments performed in the presence of ATP and Ca2+ indicate that arachidonic acid-induced Ca2+ mobilization in the nucleus takes place in a non ATP-dependent way. Taken together, these results suggest that arachidonic acid may contribute to the regulation of nuclear Ca2+ mobilization.

Adenosine Triphosphate↗

The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER.

In 8 classes of algae, namely the Cryptophyceae, Raphidophyceae, Haptophyceae, Chrysophyceae, Bacillariophyceae, Xanthophyceae, Eustigmatophyceae and Phaeophyceae, the chloroplasts, in addition to being surrounded by a double-membraned chloroplast envelope, are also enclosed by a cisterna of endoplasmic reticulum called the chloroplast ER. Often this ER cisterna is continuous with the outher membrane of the nuclear envelope in such a manner that the nuclear envelope forms a part of the ER sac enclosing the chloroplast. In all these classes of algae except the Cryptophyceae, a regular network of tubules and vesicles, named the periplastidal reticulum, is present at a specific location between the chloroplast envelope and the chloroplast ER. In the Cryptophyceae, scattered vesicles are found between the chloroplast envelope and the chloroplast ER. Ribosomes which have been shown to be arranged to polysomes are found on the outer membrane of the chloroplast ER. It is proposed that nuclear-coded proteins which are destined for the chloroplast are synthesized on these polysomes, passing during synthesis into the lumen of the ER cisterna. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles then fuse with the outer membrane of the chloroplast envelope thereby delivering their contents to the lumen of the chloroplast envelope. Proteins then cross the inner membrane of the chloroplast envelope in an as yet unknown manner. Experimental evidence for this hypothesis comes from studies on Ochromonas danica using chloramphenicol and spectinomycin, which inhibit protein synthesis on plastid ribosomes, and cycloheximide, which inhibits protein synthesis on cytoplasmic ribosomes. In cells of Ochromonas exposed to chloramphenicol or spectinomycin, the periplastidal reticulum proliferates markedly becoming several layers thick. Presumably this build up of periplastidal reticulum occurs because the transport of cytoplasmically synthesized plastid proteins is slowed down when protein synthesis in the chloroplast is inhibited. Conversely, when cells of Ochromonas are treated with cycloheximide, there is a reduction in the amount of periplastidal reticulum presumably because there are no cytoplasmically synthesized proteins to be transported into the chloroplast.

Biological Transport↗

Ultrastructure of Chilomonas paramecium and the phylogeny of the cryptoprotists.

The ultrastructure of the cryptoprotist Chilomonas paramecium is reviewed and compared to earlier accounts. Distinctive features include a complex cytoskeleton which defines the cell organization and interconnects cell components; trichocysts which resemble those in other cryptoprotists; and two non-photosynthetic plastids. During mitosis there is partial dispersal of the nuclear envelope early in prophase but some remains at the nuclear periphery throughout mitosis. At metaphase chromosomes are arranged on the longitudinal axis of an elongated elliptical nucleus. During telophase the chromosomes decondense and the nuclear envelope reforms. Cell structure is compared with that in other cryptoprotists, and origin of this taxon of algae is discussed.

Animals↗

Release of viruses and viral DNA from nucleus to cytoplasm of HeLa cells at late stages of productive adenovirus infection as revealed by electron microscope in situ hybridization.

Considerable progress has been made over the past 10 years towards a full understanding of the functional significance of the structural changes resulting from the production of adenoviruses in permissive cells. Similarly, the host-virus interactions which are involved in viral replication and gene expression as well as in RNA nuclear export have been investigated. Post-embedding nonisotopic in situ hybridization has been proven to be a powerful tool for the study of nucleic acids in infected cells provided that controlled elimination of artifacts by appropriate treatments was undertaken. Adenovirus infected cells present two biological characteristics which could lead to false positive or negative results. First, they contain large amounts of single-stranded portions of viral DNA which are revealed with viral RNA molecules. Second, DNA-binding proteins are present which hide some nucleic acid sequences. By using a DNA probe and appropriate variations in the experimental protocol, it is possible to reveal specifically different kinds of targets, simultaneously single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), or only ssDNA, or only dsDNA, or only RNA. By using two probes labeled with different haptens, biotine and digoxigenin, it is possible to detect concomitantly two nucleic acid targets and, therefore, to study their relationships. In order to gain insight into the changes in the nucleus before cell lysis and to improve our knowledge on the series of steps leading to the release of adenoviruses from the nucleus, examination of cells at 41 h post-infection and identification of structures containing adenoviral nucleic acids were undertaken. In addition to the ultrastructural changes and precise distribution of cellular DNA and viral nucleic acid molecules already described in cells up to 24 h post-infection (for a review, see Puvion E, Puvion-Dutilleul F (1996) Exp Cell Res 229, 217-225), new results were obtained. Routine observation revealed the presence of: i) viruses in the cytoplasm, some being located next to nuclear pores; ii) abnormally large portions of the nuclear envelope devoid of underlying condensed chromatin; iii) proliferation of either the inner nuclear membrane only or both membranes of the nuclear envelope; and iv) electron-opaque grains in the nuclear compartment involved in viral genome transcription, and also in the clusters of interchromatin granules known to contain mature viral messenger RNA (Bridge E et al (1996) J Cell Biol 135, 303-314). In situ hybridization revealed the presence of: i) dsDNA in the cytoplasmic viruses indicating that they were mature viruses; ii) free viral dsDNA and ssDNA molecules in the cytoplasm whereas host DNA remained confined at the nuclear border; and iii) viral RNA in the newly-described electron-opaque grains we call, therefore, viral-RNA containing grains. Immunodetection of bromodeoxyuridine (BrdU) incorporated into DNA in pulse and pulse-chase experiments allowed us to ascertain that cells at 41 h post-infection were truly living cells and that at least part of the newly-synthesized viral DNA migrated from the nucleus to the cytoplasm. Taken together, the data suggest that modifications of the nuclear matrix, cytoskeleton, and nucleo-cytoplasmic interactions might occur near the termination of adenovirus infection inducing the progressive release of viruses, vial dsDNA and ssDNA molecules in the cytoplasm. In addition, the observation of a new structural support for the intranuclear viral RNA in the clusters of interchromatin granules emphasizes the role of these cellular structures in the intranuclear trafficking of messenger RNA leading to the regulation of its nuclear export.

Adenoviruses, Human↗