Location of Subunit−Subunit Contact Sites on RNA Polymerase II Subunit 3 from the Fission YeastSchizosaccharomycespombe†

Biochemistry ◽  
1998 ◽  
Vol 37 (16) ◽  
pp. 5542-5548 ◽  
Author(s):  
Kiyoshi Yasui ◽  
Akira Ishiguro ◽  
Akira Ishihama
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Contact Sites ◽  
Subunit Contact

scholarly journals Structural basis of the nucleosome transition during RNA polymerase II passage

Science ◽  
2018 ◽  
Vol 362 (6414) ◽  
pp. 595-598 ◽  
Author(s):  
Tomoya Kujirai ◽  
Haruhiko Ehara ◽  
Yuka Fujino ◽  
Mikako Shirouzu ◽  
Shun-ichi Sekine ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Genomic Dna ◽  
Structural Basis ◽  
Histone Octamer ◽  
Contact Sites ◽  
Cryo Electron Microscopy ◽  
Nucleosomal Dna ◽  
Foreign Dna

Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo–electron microscopy structures of RNAPII-nucleosome complexes in which RNAPII pauses at the superhelical locations SHL(−6), SHL(−5), SHL(−2), and SHL(−1) of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, in which RNAPII gradually tears DNA from the histone surface while preserving the histone octamer. The nucleosomes in the SHL(−1) complexes are bound to a “foreign” DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.

scholarly journals Mapping the  70 subunit contact sites on Escherichia coli RNA polymerase with a  70-conjugated chemical protease

1998 ◽  
Vol 95 (11) ◽  
pp. 6021-6026 ◽  
Author(s):  
J. T. Owens ◽  
R. Miyake ◽  
K. Murakami ◽  
A. J. Chmura ◽  
N. Fujita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Contact Sites ◽  
Subunit Contact

scholarly journals Molecular Assembly of the Influenza Virus RNA Polymerase: Determination of the Subunit-Subunit Contact Sites

1996 ◽  
Vol 77 (9) ◽  
pp. 2149-2157 ◽  
Author(s):  
T. Toyoda ◽  
D. M. Adyshev ◽  
M. Kobayashi ◽  
A. Iwata ◽  
A. Ishihama
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Molecular Assembly ◽  
Contact Sites ◽  
Virus Rna ◽  
Subunit Contact

Nutrient-regulated gene expression in eukaryotes

2006 ◽  
Vol 73 ◽  
pp. 85-96 ◽  
Author(s):  
Richard J. Reece ◽  
Laila Beynon ◽  
Stacey Holden ◽  
Amanda D. Hughes ◽  
Karine Rébora ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Control ◽  
Direct Interaction ◽  
Signalling Pathways ◽  
A Cell ◽  
One Step ◽  
Higher Eukaryotes ◽  
Regulated Gene Expression

The recognition of changes in environmental conditions, and the ability to adapt to these changes, is essential for the viability of cells. There are numerous well characterized systems by which the presence or absence of an individual metabolite may be recognized by a cell. However, the recognition of a metabolite is just one step in a process that often results in changes in the expression of whole sets of genes required to respond to that metabolite. In higher eukaryotes, the signalling pathway between metabolite recognition and transcriptional control can be complex. Recent evidence from the relatively simple eukaryote yeast suggests that complex signalling pathways may be circumvented through the direct interaction between individual metabolites and regulators of RNA polymerase II-mediated transcription. Biochemical and structural analyses are beginning to unravel these elegant genetic control elements.

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