Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequences

Allegra, Paola; Sterner, Richard; Clayton, David F.; Allfrey, Vincent G.

doi:10.1016/0022-2836(87)90698-x

Cited by 170 publications

(96 citation statements)

References 79 publications

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“…"Split" nucleosomes generated this way were supposed to have a role in transcription. In fact, it is evident from a number of studies that activation of chromatin is accompanied by exposure of the normally buried cysteines of H3 (Prior et al, 1983;Cocco et al, 1986;Allegra et al, 1987;Chen & Allfrey, 1987;Johnson et al, 1987). Because changes leading to the opening of nucleosome structure are thought to be involved in activation of chromatin, a nucleosome carrying a fluorescence probe at its H3 molecules can also be considered as having a conformation close to that of the nucleosome of active chromatin.…”

Section: Discussionmentioning

confidence: 99%

Dynamics of interaction of RNA polymerase II with nucleosomes. II. During read‐through and elongation

Bhargava

1993

Protein Science

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The sulfhydryl-specific fluorescence probe 1,SIAEDANS (5-(2-((iodoacetyl)amino)ethyl)amino-naphthalene-1-sulfonic acid) was attached to the single cysteine of H3, and reconstituted fluorescent mononucleosomes were used as the template for in vitro transcription by the yeast RNA polymerase I1 (pol 11). DNase 1 digestion analysis revealed that transcription of nucleosomes by pol I1 resulted in an overall loosening of the structure. Monitoring the transcription event by steady-state fluorescence analysis showed that nucleosomes only partially open during transcription. This opening is transient in nature, and nucleosomes close back as soon as the pol I1 falls off the template. Thus, using the technique of fluorescence spectroscopy, partial opening of nucleosome structure could be differentiated from complete dissociation into free DNA and histone octamer, a distinction that may not be possible by techniques like gel electrophoresis. Time-resolved fluorescence emission spectroscopy suggested that during read-through of the template by the pol 11, histone octamers do not fall off the DNA. Only minor conformational changes within the histone octamer take place to accommodate the transcribing polymerase.

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Section: Discussionmentioning

confidence: 99%

Dynamics of interaction of RNA polymerase II with nucleosomes. II. During read‐through and elongation

Bhargava

1993

Protein Science

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“…Therefore, a specific histone deacetylase would be able to generate additional positive charge in specific areas of such chromatin. According to our proposal, H2A and H2B, apart from being minor substrates for histone acetyltransferases, have to be rapidly deacetylated by a specific histone deacetylase when early transcriptional activa-Volume 317, number 3 February 1993 tion occurs. Our recent finding of HDlA phosphorylation with the resulting increase in H2A specificity suggests that identical pathways of intracellular signal transduction, which are generally involved in the activation of genes, could regulate the substrate specificity of the deacetylase via phosphorylation/dephosphorylation mechanisms.…”

Section: Hypothesismentioning

confidence: 98%

Histone deacetylase

et al. 1993

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Core histones can be modified by reversible, posttranslational acetylation of specific lysine residues within the N-terminal protein domains. The dynamic equilibrium of acetylation is maintained by two enzyme activities, histone acetyltransferase and histone deacetylase. Recent data on histone deacetylases and on anionic motifs in chromatin-or DNA-binding regulatory proteins (e.g. transcription factors, nuclear proto-oncogenes) are summarized and united into a hypothesis which attributes a key function to histone deacetylation for the binding of regulatory proteins to chromatin by a transient, specific local increase of the positive charge in the N-terminal domains of nucleosomal core histones. According to our model, the rapid deacetylation of distinct lysines in especially H2A and H2B would facilitate the association of anionic protein domains of regulatory proteins to specific nucleosomes. Therefore histone deacetylation (histone deacetylases) may represent a unique regulatory mechanism in the early steps of gene activation, in contrast to the more structural role of histone acetylation (histone acetyltransferases) for nucleosomal transitions during the actual transcription process.

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“…For example, most genes require acetylation of lysine residues in the N-terminal tails of histones H3 and H4 for full transcriptional activation. 110,111 Histone acetylation is observed during immediate early gene activation, [112][113][114][115][116] and localization of several proteins with histone acetylation activity to specific IE gene promotors has been reported, including CBP (CREB binding protein), p300, or PCAF (p300/CBP-associated factor). 117 Whereas it had been initially suggested that H3S10ph could directly enhance subsequent histone acetylation by increasing the binding affinity of the histone tail for HAT complexes, 115,118,119 recent results question such a simple interpretation.…”

Section: Hp1 Switchng In Other Contexts?mentioning

confidence: 99%

Dynamic Regulation of Effector Protein Binding to Histone Modifications: The Biology of HP1 Switching

Dormann¹,

Tseng²,

Allis³

et al. 2006

Cell Cycle

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Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequences

Cited by 170 publications

References 79 publications

Dynamics of interaction of RNA polymerase II with nucleosomes. II. During read‐through and elongation

Dynamics of interaction of RNA polymerase II with nucleosomes. II. During read‐through and elongation

Histone deacetylase

Dynamic Regulation of Effector Protein Binding to Histone Modifications: The Biology of HP1 Switching

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