RNA polymerase activity and template activity of chromatin after butyrate induced hyperacetylation of histones in<i>Physarum</i>

Loidl, Peter; Loidl, Adele; Puschendorf, Bernd; Gröbner, Peter

doi:10.1093/nar/12.13.5405

Cited by 20 publications

(12 citation statements)

References 48 publications

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“…We have previously demonstrated that there is no unique correlation between the steady state level of H4 acetylation and transcription during the cell cycle (7). Furthermore we did not observe a difference in the template activity of chromatin for in vitro transcription, when we compared normal Physarum chromatin with chromatin hyperacetylated by butyrate in vivo (8).…”

Section: Introductionmentioning

confidence: 62%

“…Thus, protamine is able to displace core histones from DNA better in S-chromatin as compared to G2-chromatin. To explore whether a specifically elevated acetylation state (as represented by the S-phase chromatin) is responsible for a facilitated histone release or just an unspecific elevation of the acetylation state, as observed after butyrate-induced hyperacetylation (7,8), we compared control chromatin with chromatin from butyrate-treated plasmodia. Butyrate-S-chromatin differs strikingly from control-S-chromatin.…”

Section: Resultsmentioning

confidence: 99%

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Postsynthetic acetylation of histones during the cell cycle: a general function for the displacement of histones during chromatin rearrangements

Loidl

Gröbner²

1987

Nucl Acids Res

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Postsynthetic acetylation of core histones exhibits a peak during S-phase of the Physarum cell cycle. The maximum 3H-acetate incorporation precedes the maximum of histone synthesis. Acetate is incorporated into all core histones during S-phase, but only into H2A and H2B during G2-period. Resolution of acetylated H4-subspecies reveals acetate incorporation into preexisting H4, but not into newly synthesized molecules during mitosis and early S-phase. In a protamine competition assay histones from S-phase chromatin are released at lower protamine concentrations as compared to the lower acetylated G2-chromatin. We demonstrate a preferential release of highly acetylated H4-subspecies at low protamine concentrations. Our results fit into a general model of the relationship between histone acetylation and chromatin assembly. According to this model acetylation of core histones would serve as a signal for displacement of histones from nucleosomes by modulating histone-protein or histone-DNA interactions. We propose that this mechanism operates during DNA-replication and transcription, as well as during other chromatin rearrangements.

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Section: Introductionmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 99%

Postsynthetic acetylation of histones during the cell cycle: a general function for the displacement of histones during chromatin rearrangements

Loidl

Gröbner²

1987

Nucl Acids Res

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“…Previous work from our laboratory has shown a lack of correlation between histone acetylation and the transcriptional activity of chromatin in Physarum [2,3]. Recent results on the functional role of histone acetylation suggest that it serves as a general mechanism in the displacement of histones during structural transitions of chromatin [4].…”

Section: Introductionmentioning

confidence: 89%

“…Histones, the main structural proteins of eucaryotic chromatin, undergo various reversible, postsynthetic modifications, among which acetylation of e-amino groups of lysine residues has been extensively studied [1]. Previous work from our laboratory has shown a lack of correlation between histone acetylation and the transcriptional activity of chromatin in Physarum [2,3]. Recent results on the functional role of histone acetylation suggest that it serves as a general mechanism in the displacement of histones during structural transitions of chromatin [4].…”

Section: Introductionmentioning

confidence: 99%

Histone acetyltransferase activity during the cell cycle

Golderer¹,

Loidl²,

Gröbner³

1987

FEBS Letters

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Histone acetyltransferase activity was measured in isolated nuclei during the synchronous cell cycle of the myxomycete Physarum polycephalum. Nuclei were incubated with p4C]acetyl-coenzyme A and an excess of exogenous calf thymus histones. The activity is periodic during the cell cycle; it rises during the S-phase to reach a maximum in the early G2-period with a decline in mid and late G 2. Comparison of the pattern of enzyme activity with the in vivo acetylation of histones during the cell cycle reveals that the enzyme activity does not wholly determine the acetylation state, indicating that other factors, including possibly the structural state of chromatin, are responsible for the observed cell cycle pattern of in vivo histone acetylation.

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“…This toxic substance might inhibit growth by inhibition of acetyl-CoA synthesis (La Rossa et al 1987) or by a subsequent building up of ␣-amino-n-butyrate, another toxic BAA intermediate (Rhodes et al 1987). There is evidence that ␣-amino-nbutyrate can inhibit cell division in Allium root tips (Langzagorta et al 1988), acetylate histones in Physarum (Loidl et al 1984), and stop cell division in Hordeum roots tips by acidifying the cytoplasm (Reid et al 1985).…”

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confidence: 99%

Some Effects of Chlorsulfuron on the Ultrastructure of Root and Leaf Cells in Pea Plants

Stoynova

Petrov

Semerdjieva

1997

J Plant Growth Regul

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Roots of intact pea plants were treated with 2.8 × 10 −4 M Chlorsulfuron (CS). Meristematic root cells and leaf mesophyll cells were studied. Mitochondria, nucleoli, and chloroplasts were the first cell compartments to show ultrastructural disturbances. Mitochondria in treated plants had a visibly translucent matrix. The nucleoli were in the process of segregation of their fibrillar and granular components and reduction of their volume. The structural disturbances of the chloroplasts were similar to those observed during senescence. The results support the hypothesis that CS inhibits cell growth through the accumulation of toxic intermediates.

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RNA polymerase activity and template activity of chromatin after butyrate induced hyperacetylation of histones inPhysarum

Abstract: We have studied the effect of sodium-n-butyrate on endogenous RNA polymerase in Physarum polycephalum.

Cited by 20 publications

References 48 publications

Postsynthetic acetylation of histones during the cell cycle: a general function for the displacement of histones during chromatin rearrangements

Postsynthetic acetylation of histones during the cell cycle: a general function for the displacement of histones during chromatin rearrangements

Histone acetyltransferase activity during the cell cycle

Some Effects of Chlorsulfuron on the Ultrastructure of Root and Leaf Cells in Pea Plants

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