Fate of linear and supercoiled multinucleosomic templates during transcription.

Détails

ID Serval
serval:BIB_742E8D2F31B7
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Fate of linear and supercoiled multinucleosomic templates during transcription.
Périodique
EMBO Journal
Auteur(s)
ten Heggeler-Bordier B., Schild-Poulter C., Chapel S., Wahli W.
ISSN
0261-4189[print], 0261-4189[linking]
Statut éditorial
Publié
Date de publication
06/1995
Volume
14
Numéro
11
Pages
2561-2569
Langue
anglais
Notes
Publication types: In Vitro ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Electron microscopy was used to monitor the fate of reconstituted nucleosome cores during in vitro transcription of long linear and supercoiled multinucleosomic templates by the prokaryotic T7 RNA polymerase and the eukaryotic RNA polymerase II. Transcription by T7 RNA polymerase disrupted the nucleosomal configuration in the transcribed region, while nucleosomes were preserved upstream of the transcription initiation site and in front of the polymerase. Nucleosome disruption was independent of the topology of the template, linear or supercoiled, and of the presence or absence of nucleosome positioning sequences in the transcribed region. In contrast, the nucleosomal configuration was preserved during transcription from the vitellogenin B1 promoter with RNA polymerase II in a rat liver total nuclear extract. However, the persistence of nucleosomes on the template was not RNA polymerase II-specific, but was dependent on another activity present in the nuclear extract. This was demonstrated by addition of the extract to the T7 RNA polymerase transcription reaction, which resulted in retention of the nucleosomal configuration. This nuclear activity, also found in HeLa cell nuclei, is heat sensitive and could not be substituted by nucleoplasmin, chromatin assembly factor (CAF-I) or a combination thereof. Altogether, these results identify a novel nuclear activity, called herein transcription-dependent chromatin stabilizing activity I or TCSA-I, which may be involved in a nucleosome transfer mechanism during transcription.
Mots-clé
Animals, Cell Nucleus/metabolism, DNA, Superhelical/genetics, DNA, Superhelical/metabolism, DNA-Directed RNA Polymerases/metabolism, Hela Cells, Humans, Liver/metabolism, Microscopy, Electron, Nuclear Proteins/metabolism, Nucleoplasmins, Nucleosomes/metabolism, Nucleosomes/ultrastructure, Phosphoproteins, Plasmids/genetics, Plasmids/metabolism, RNA Polymerase II/metabolism, Rats, Transcription, Genetic, Viral Proteins
Pubmed
Web of science
Création de la notice
24/01/2008 17:05
Dernière modification de la notice
03/03/2018 18:21
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