Subunit structures of different electrophoretic forms of nucleosomes.

Albright, S C; Wiseman, John M.; Lange, Richard A.; Garrard, William T.

doi:10.1016/s0021-9258(19)85757-5

Cited by 143 publications

(36 citation statements)

References 44 publications

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“…This result would imply that histone-DNA contacts might exist over as much as 180 bp of DNA. That such extensive interaction may occur has been previously suggested following analysis of histone-DNA contacts in linker DNA (Karpov et al, 1982;Bavykin et al, 1990) and micrococcal nuclease digestion analysis of chromatin depleted of linker histones (Todd & Garrard, 1977;Albright et al, 1980).…”

Section: Resultsmentioning

confidence: 84%

Histone-DNA contacts in a nucleosome core containing a Xenopus 5S rRNA gene

Pruss¹,

Wolffe²

1993

Biochemistry

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We describe histone-DNA cross-linking in a nucleosome core containing a Xenopus borealis somatic 5S rRNA gene. Histones H3 and H4 are cross-linked to DNA within 30 bp to either side of the dyad axis. Histones H2A/H2B and H3 are cross-linked to DNA where it enters and exists, wrapping around the histone octamer. These latter interactions extend for 80 bp to one side of the dyad axis of the nucleosome core, including the entire binding site for transcription factor TFIIIA. These extensive interactions with linker DNA might account for inhibition of TFIIIA binding and also might assist in the folding of internucleosomal DNA within the chromatin fiber.

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Section: Resultsmentioning

confidence: 84%

Histone-DNA contacts in a nucleosome core containing a Xenopus 5S rRNA gene

Pruss¹,

Wolffe²

1993

Biochemistry

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“…Isotope Labeling: Cells to be labeled in the presence of ara-C were preincubated with the drug (Siama) at 25-50 ig/m.l for 1 hour, unless otherwise indicated. Cells were concentrated approximately 20-fold and incubated with label (3t-lysine, 68 Ci/mmol, 10-100 pCi/ml; 3L-uridine, 30 Ci/mmol, 10 pCi/ml; 3H-amino acid mixture, 10 pCi/ml; 3d-thymidine, 70 Ci/mmol, 10-400 pCi/mI) in the conditioned mediurn. RadioLabeled amino acids, thymidine and uridine were purchlased from New England Nuclear or Amershiam.…”

Section: Methodsmentioning

confidence: 99%

“…To examine the chromatin binding of proteins synthesized in ara-C, nucleoprotein samples were subjected to low ionic strength gel electrophoresis. The electrophoretic separation of chromatin fragments is more sensitive to protein content and net particle charge than DNA fragment length per se (30,31,32,33). The electrophoretic pattern of nucleosome particles generated from cells labeled with 3H-thymidine in ara-C resembles the control pattern (Figure 3).…”

Section: Drug Effects On Precursor Incorporationmentioning

confidence: 99%

Chromatin assembled in the presence of cytosine arabinoside has a short nucleosome repeat

Leffak

1983

Nucl Acids Res

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Incubation of MSB cells with cytosine arabinoside (1-beta-D-arabinofuranosylcytosine, ara-C) inhibits 3H-thymidine incorporation into nascent DNA while nucleosome core histone synthesis proceeds in molar stoichiometry at about 20% of control rates. The excess nascent histone is incorporated into chromatin and nucleosome cores are assembled normally on the small amount of DNA which is synthesized at submaximal levels of ara-C. This DNA becomes packaged into a shortened nucleosome repeat, however. These results indicate that the nucleosome core is a strongly conserved unit of chromatin replication and suggest that the stoichiometry of nascent histone to DNA may be one factor influencing the establishment of the nucleosome repeat length. It cannot be the only factor, however, since the closely packed nucleosomes made in the presence of ara-C begin to return to their normal spacing within six hours after reversal.

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“…Nucleoprotein Organization during Chromatin Maturation. Nucleosomal monomers can be fractionated by gel electrophoresis as a function of their protein composition and DNA length (Levinger & Varshavsky, 1980;Albright et al, 1980). Therefore, we used this technique to analyze the nucleoprotein products from MNase digestion of replicating SV40 [32P]chromatin that was pulse labeled in vitro (Figure 8A,B,E), mature SV40 [32P] chromatin that was formed in vitro during a chase period (Figure 8C,F), and mature SV40 [3H]chromatin that was formed in intact cells (Figure 8D), In each case, hypotonic nuclear extracts were prepared from virusinfected cells.…”

Section: Resultsmentioning

confidence: 99%

“…MNase were similar to multiple forms of nucleosomal monomers previously described for mammalian chromosomes (Albright et al, 1980;Levinger & Varshavsky, 1980;Annunziato et al, 1981;Schlaeger, 1982). We refer to these as Ml, M2, and M3.…”

Section: The Most Easily Recognized Nucleoproteins Released Bymentioning

confidence: 98%

Structure of chromatin at deoxyribonucleic acid replication forks: nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure

Cusick¹,

Lee²,

DePamphilis³

et al. 1983

Biochemistry

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Relative to nonreplicating DNA in mature simian virus 40 (SV40) chromosomes, newly synthesized DNA in replicating SV40 chromosomes was found to be hypersensitive to the nonspecific endonucleases, micrococcal nuclease (MNase), DNase I, and DNase II. Nascent DNA, pulse labeled in either intact cells or nuclear extracts supplemented with cytosol, was digested about 5-fold faster and about 25% more extensively than uniformly labeled DNA in mature viral chromosomes. Pulse-chase experiments in vitro revealed a time-dependent chromatin maturation process that involved two distinct steps: (i) conversion of prenucleosomal DNA (PN-DNA) into immature nucleosomal oligomers and (ii) maturation of newly assembled chromatin into a structure with increased nuclease resistance. PN-DNA was hypersensitive to MNase, releasing short DNA fragments which were subsequently solubilized by the nuclease. However, when the nascent PN-DNA was specifically removed by digestion of replicating viral chromosomes with Escherichia coli exonuclease III (3'-5') and phage T7 exonuclease (5'-3'), subsequent digestion of the remaining chromatin with MNase revealed the same degree of hypersensitivity observed prior to exonuclease treatment. Furthermore, newly assembled nucleosomal oligomers, isolated after a brief MNase digestion of replicating viral chromosomes, were also hypersensitive to MNase relative to oligomers isolated from mature chromosomes. Hybridization analysis of the DNA in these immature oligomers revealed that it originated from both sides of replication forks. Inhibition of DNA polymerase alpha by aphidicolin inhibited conversion of PN-DNA into nucleosomes but did not inhibit loss of nucleosomal hypersensitivity to MNase. In contrast, components in the soluble fraction of the subcellular system ("cytosol") were required for both DNA replication and chromatin maturation. Analysis of the nucleoprotein products from a MNase digestion of replicating and mature SV40 chromosomes failed to detect a change in nucleosome structure that corresponded to the loss of nuclease hypersensitivity. However, the results presented demonstrate that both PN-DNA and newly assembled immature chromatin, present on both arms of SV40 replication forks, contribute to the commonly observed hypersensitivity of newly replicated chromatin to endonucleases.

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Subunit structures of different electrophoretic forms of nucleosomes.

Cited by 143 publications

References 44 publications

Histone-DNA contacts in a nucleosome core containing a Xenopus 5S rRNA gene

Histone-DNA contacts in a nucleosome core containing a Xenopus 5S rRNA gene

Chromatin assembled in the presence of cytosine arabinoside has a short nucleosome repeat

Structure of chromatin at deoxyribonucleic acid replication forks: nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure

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