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Synergistic action of RNA polymerases in overcoming the nucleosomal barrier
- Source :
- Nature structural & molecular biology
- Publication Year :
- 2009
-
Abstract
- During gene expression, RNA polymerase (RNAP) encounters a major barrier at a nucleosome and yet must access the nucleosomal DNA. Previous in vivo evidence has suggested that multiple RNAPs might increase transcription efficiency through nucleosomes. Here we have quantitatively investigated this hypothesis using Escherichia coli RNAP as a model system by directly monitoring its location on the DNA via a single-molecule DNA-unzipping technique. When an RNAP encountered a nucleosome, it paused with a distinctive 10-base pair periodicity and backtracked by approximately 10-15 base pairs. When two RNAPs elongate in close proximity, the trailing RNAP apparently assists in the leading RNAP's elongation, reducing its backtracking and enhancing its transcription through a nucleosome by a factor of 5. Taken together, our data indicate that histone-DNA interactions dictate RNAP pausing behavior, and alleviation of nucleosome-induced backtracking by multiple polymerases may prove to be a mechanism for overcoming the nucleosomal barrier in vivo.
- Subjects :
- DNA, Bacterial
Transcription, Genetic
genetic processes
RNA-dependent RNA polymerase
RNA polymerase II
Biology
Models, Biological
Article
Histones
03 medical and health sciences
chemistry.chemical_compound
Structural Biology
RNA polymerase
RNA polymerase I
Escherichia coli
Molecular Biology
RNA polymerase II holoenzyme
Polymerase
030304 developmental biology
0303 health sciences
Escherichia coli Proteins
030302 biochemistry & molecular biology
RNA
DNA-Directed RNA Polymerases
Molecular biology
Cell biology
Nucleosomes
enzymes and coenzymes (carbohydrates)
chemistry
RNA editing
biology.protein
health occupations
bacteria
RNA Polymerase II
Subjects
Details
- ISSN :
- 15459985
- Volume :
- 17
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Nature structuralmolecular biology
- Accession number :
- edsair.doi.dedup.....8b9a49e3d379722d7b9eb3361e0862af