Helicobacter pylori RNA polymerase α-subunit C-terminal domain shows features unique to ɛ-proteobacteria and binds NikR/DNA complexes-Reference-Cited by-同舟云学术

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Helicobacter pylori RNA polymerase α-subunit C-terminal domain shows features unique to ɛ-proteobacteria and binds NikR/DNA complexes

Published:2014-02-04 Issue:4 Volume:23 Page:454-463
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Borin Brendan N.¹,Tang Wei²,Krezel Andrzej M.¹²³

Affiliation:

1. Department of Biological Sciences; Vanderbilt University; Nashville Tennessee 37232

2. Department of Biochemistry and Molecular Biophysics; Washington University School of Medicine; St. Louis Missouri 63110

3. Department of Pathology and Immunology; Washington University School of Medicine; St. Louis Missouri 63110

Funder

NIH

NIH Molecular Biophysics Training Program

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2427/fullpdf

Reference40 articles.

1. The evolving story of the omega subunit of bacterial RNA polymerase;Mathew;Trends Microbiol,2006

2. Urea sensitization caused by separation of Helicobacter pylori RNA polymerase beta and beta' subunits;Dailidiene;Helicobacter,2007

3. The major sigma factor (RpoD) from Helicobacter pylori and other gram-negative bacteria shows an enhanced rate of divergence;Solnick;J Bacteriol,1997

4. Flexible linker in the RNA polymerase alpha subunit facilitates the independent motion of the C-terminal activator contact domain;Jeon;J Mol Biol,1997

5. Functional specialization within the alpha-subunit of Escherichia coli RNA polymerase;Hayward;J Mol Biol,1991

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