In Vitro Transcription of Chromatin Containing Histones Hyperacetylated in Vivo

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1980 Sep 25

PMID 7001364

Citations 9

Authors

M E Dobson

V M Ingram

Affiliations

Soon will be listed here.

Abstract

The culture of cells in the presence of sodium n-butyrate causes an accumulation of histones that are highly acetylated. When chromatin containing these histones was transcribed with E. coli RNA polymerase, an increase in the template activity compared to control chromatin was observed. Titration of chromatin with polymerase under both reinitiating and non-reinitiating conditions showed there was no increase in the number of regions available for transcription. Comparison of the kinetics for single and multiple rounds of transcription indicated that the rate of elongation was increased and probably the rate of reinitiation as well. Comparison of the size of transcripts from control and acetylated chromatin showed a small increase in the average size of transcripts from acetylated chromatin. When transcription was compared using partially purified HeLa polymerase, an increase was also seen. Studies under various ionic conditions showed that control chromatin required a higher salt concentration for optimum activity than did acetylated chromatin. In addition, at the optimum salt concentration for each chromatin, there was very little difference in the transcriptional activity using exogenous HeLa RNA polymerase.

Citing Articles

Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II.

Oishi T, Hatazawa S, Kujirai T, Kato J, Kobayashi Y, Ogasawara M Nucleic Acids Res. 2023; 51(19):10364-10374.

PMID: 37718728 PMC: 10602921. DOI: 10.1093/nar/gkad754.

Transcription of mononucleosomal particles acetylated in the presence of n-butyrate.

Pineiro M, Hernandez F, Puerta C, Palacian E Mol Biol Rep. 1993; 18(1):37-41.

PMID: 8232292 DOI: 10.1007/BF01006893.

Histone modifications in the yeast S. Cerevisiae.

Davie J, Saunders C, Walsh J, Weber S Nucleic Acids Res. 1981; 9(13):3205-16.

PMID: 7024912 PMC: 327343. DOI: 10.1093/nar/9.13.3205.

Histone hyperacetylation has little effect on the higher order folding of chromatin.

McGhee J, Nickol J, Felsenfeld G, Rau D Nucleic Acids Res. 1983; 11(12):4065-75.

PMID: 6866766 PMC: 326025. DOI: 10.1093/nar/11.12.4065.

Acetylation of histones in nucleosomes.

Doenecke D, Gallwitz D Mol Cell Biochem. 1982; 44(2):113-28.

PMID: 6808351 DOI: 10.1007/BF00226895.

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