Chromatin-Like Structures in Polyoma Virus and Simian Virus 40 Lytic Cycle

Crémisi, C; Pignatti, Pier Franco; Croissant, O; Yaniv, Moshe

doi:10.1128/jvi.17.1.204-211.1976

Cited by 161 publications

(58 citation statements)

References 31 publications

(34 reference statements)

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“…An average of 23 beads per ring with a mean diameter of 100 nm has been determined on the 5.2 kb long DNA circle. The compaction ratio of 2.8 in this extended configuration is in good agreement with values determined for SV40 minichromosomes under similar spreading conditions (Griffith, 1975;Cremisi et al, 1976). The lower magnification in Figure Sc gives a representative overview of several assembled DNA molecules, and demonstrates the overall dense packaging of the DNA into nucleosomes.…”

Section: Nucleosome Assembly Activity Of the Purified Histone Complexessupporting

confidence: 86%

Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.

1990

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High speed supernatants of Xenopus laevis oocyte nuclei efficiently assemble DNA into nucleosomes in vitro under physiological salt conditions. The assembly activity cofractionates with two histone complexes composed of the acidic protein N1/N2 in complex with histones H3 and H4, and nucleoplasmin in complex with histones H2B and H2A. Both histone complexes have been purified and their nucleosome assembly activities have been analysed separately and in combination. While the histones from the N1/N2 complexes are efficiently transferred to DNA and induce supercoils into relaxed circular plasmid DNA, the nucleoplasmin complexes show no supercoil induction, but can also transfer their histones to DNA. In combination, the complexes act synergistically in supercoil induction thereby increasing the velocity and the number of supercoils induced. Electron microscopic analysis of the reaction products shows fully packaged nucleoprotein structures with the typical nucleosomal appearance resulting in a compaction ratio of 2.8 under low ionic strength conditions. The high mobility group protein HMG‐1, which is also present in the soluble nuclear homogenate from X. laevis oocytes, is not required for nucleosome core assembly. Fractionation experiments show that the synergistic effect in the supercoiling reaction can be exerted by histones H3 and H4 bound to DNA and the nucleoplasmin complexes alone. This indicates that it is not the synchronous action of both complexes which is required for nucleosome assembly, but that their cooperative action can be resolved into two steps: deposition of H3 and H4 from the N1/N2 complexes onto the DNA and completion of nucleosome core formation by addition of H2B and H2A from the nucleoplasmin complexes.

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Section: Nucleosome Assembly Activity Of the Purified Histone Complexessupporting

confidence: 86%

Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.

1990

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“…This is the first structural description of such a structure in virus-infected plants. The structure is similar to those of SV40 DNA (Griffith, 1975;Bellard et al, 1976) and polyoma minichromosomes (Cremisi et al, 1976). Our results are in good agreement with those obtained by micrococcal nuclease digestion (Olszewski et al, 1982).…”

Section: Discussionsupporting

confidence: 88%

Electron microscopic studies of the different topological forms of the cauliflower mosaic virus DNA: knotted encapsidated DNA and nuclear minichromosome.

Menissier¹,

Murcia²,

Lebeurier³

et al. 1983

The EMBO Journal

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Cauliflower mosaic virus (CaMV) DNA exists under different topological forms in infected plants. First, the population of encapsidated CaMV DNA molecules appears heterogeneous when analysed by gel electrophoresis. The electron microscopic study reported here reveals that CaMV virion DNA contains simple and multiple topological knots. Second, a supercoiled DNA form never found in virions exists as a chromatin‐like nucleoprotein complex with nucleosome subunits in the nuclei of infected leaves. The compaction ratio of the minichromosomes is compatible with the nucleosomal structure, the number of nucleosomes (41.0 +/‐ 2.5) is in keeping with the length of the viral genome.

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“…In these respects the SV40 chromatin was similar to chromatin isolated from a variety of mammalian cells (8). We assume that the DNA regions inaccessible to extensive staphylococcal nuclease digestion (6) are contained in the nucleohistone complexes (nucleosomes or v-bodies) seen by electron microscopy (9,12).…”

Section: Discussionmentioning

confidence: 80%

“…It has been demonstrated that the histones of SV40 chromatin isolated from infected cells (9,12) or from visions (5) are condensed into 21 spherical units or v-bodies. It is presumably these structures that result in the failure of staphylococcal nuclease to digest completely all ofthe DNA ofchromatin.…”

mentioning

confidence: 99%

Interaction of Simian Virus 40 chromatin with Simian Virus 40 T-antigen

Persico-Dilauro¹,

Martin²,

Livingston³

1977

J Virol

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We have studied the binding of the tumor antigen (T-antigen) of simian virus 40 to simian virus 40 chromatin (minichromosomes). The minichromosomes isolated from infected cells by a modification of standard techniques were relatively free of contaminating RNA and cellular DNA and had a ratio (by weight) of protein to DNA of approximately 1; their DNA was 50 to 60% digestible to an acid-soluble form by staphylococcal nuclease. Cleavage of this chromatin with restriction endonucleases indicated that the nuclease-resistant regions were randomly distributed in the population of minichromosomes, but were not randomly distributed within minichromosomes. Only 20 to 35% of these minichromosomes adsorbed nonspecifically to nitrocellulose filters, permitting binding studies between simian virus 40 T-antigen and chromatin to be performed. Approximately two to three times as much T-antigen was required to bind chromatin as to bind an equivalent amount of free DNA. When T-antigen was present in excess, both chromatin and free DNA were quantitatively retained on the filters. On the other hand, when DNA or chromatin was present in excess, only one-third as much chromatin as DNA was retained. We suggest that T-antigen-chromatin complexes may be formed by the cooperative binding of T-antigen to chromatin, whereas T-antigen-DNA complexes may be formed by simple bimolecular interactions.The tumor antigen (T-antigen) of simian virus 40 (SV40), encoded by the viralA gene (1,18,23,24,32), binds to SV40 DNA (3) and is required for the initiation of viral DNA synthesis (4, 31). DNA replication is initiated at a unique site located 0.67 fractional unit from the EcoRI site on the conventional physical map of SV40 (11). Curiously, however, T-antigen binds with high affinity to three different HindII + HI restriction fragments of SV40 DNA, only one of which includes the origin of DNA replication (16). We have therefore examined the interaction of Tantigen with SV40 chromatin to determine whether the condensation of DNA into chromatin affected its capacity to bind T-antigen.It has been demonstrated that the histones of SV40 chromatin isolated from infected cells (9, 12) or from visions (5) are condensed into 21 spherical units or v-bodies. It is presumably these structures that result in the failure of staphylococcal nuclease to digest completely all ofthe DNA ofchromatin. Polisky and McCarthy (26) have argued that the protected regions are randomly distributed along the DNA; however, the chromatin they studied was prepared from virions by a technique that disrupts the v-bodies (5). We have therefore reexamined the distribution of the protected regions preparatory to the study of T-antigen binding to chromatin. MATERIALS AND ME]HODSCell growth. BSC-1 monkey kidney cells were grown in 75-cm2 tissue culture flasks (Falcon Plastics, Oxnard, Calif.) or 700-cm2 glass roller bottles in Eagle minimal essential medium (MEM; NIH Media Supply) supplemented with 2% (MEM-2) or 10% (MEM-10) fetal bovine serum (Flow Laboratories, Inc., Rockville, Md.) in ...

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Chromatin-Like Structures in Polyoma Virus and Simian Virus 40 Lytic Cycle

Cited by 161 publications

References 31 publications

Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.

Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.

Electron microscopic studies of the different topological forms of the cauliflower mosaic virus DNA: knotted encapsidated DNA and nuclear minichromosome.

Interaction of Simian Virus 40 chromatin with Simian Virus 40 T-antigen

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