scholarly journals Identification of a mutation within the structural gene for the α subunit of DNA-dependent RNA polymerase of E. Coli

1976 ◽  
Vol 147 (1) ◽  
pp. 119-119
Author(s):  
H. Fujiki ◽  
P. Palm ◽  
W. Zillig ◽  
R. Calendar ◽  
M. Sunshine
Keyword(s):  
Rna Polymerase ◽  
Structural Gene ◽  
Α Subunit ◽  
E Coli

Interaction of the C-terminal domain of the E. coli RNA polymerase α subunit with the UP element: recognizing the backbone structure in the minor groove surface11Edited by R. Ebright

2001 ◽  
Vol 306 (2) ◽  
pp. 213-225 ◽  
Author(s):  
Kazuhiro Yasuno ◽  
Toshio Yamazaki ◽  
Yoshiyuki Tanaka ◽  
Takashi S Kodama ◽  
Akimasa Matsugami ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Minor Groove ◽  
Α Subunit ◽  
E Coli ◽  
Terminal Domain ◽  
Backbone Structure

scholarly journals NusA Interaction with the α Subunit of E. coli RNA Polymerase Is via the UP Element Site and Releases Autoinhibition

Structure ◽  
2011 ◽  
Vol 19 (7) ◽  
pp. 945-954 ◽  
Author(s):  
Kristian Schweimer ◽  
Stefan Prasch ◽  
Pagadala Santhanam Sujatha ◽  
Mikhail Bubunenko ◽  
Max E. Gottesman ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Α Subunit ◽  
E Coli

ELECTROSTATIC PROPERTIES OF PROMOTER RECOGNIZED BYE. COLIRNA POLYMERASE Eσ70

2006 ◽  
Vol 04 (02) ◽  
pp. 455-467 ◽  
Author(s):  
ANATOLY A. SOROKIN ◽  
ALEXANDR A. OSYPOV ◽  
TIMUR R. DZHELYADIN ◽  
PETR M. BESKARAVAINY ◽  
SVETLANA G. KAMZOLOVA
Keyword(s):  
Escherichia Coli ◽  
Comparative Analysis ◽  
Rna Polymerase ◽  
Α Subunit ◽  
Promoter Sequences ◽  
E Coli ◽  
Adp Ribosylation ◽  
Electrostatic Properties ◽  
Differential Recognition ◽  
T4 Phage

A comparative analysis of electrostatic patterns for 359 σ70-specific promoters and 359 nonpromoter regions on electrostatic map of Escherichia coli genome was carried out. It was found that DNA is not a uniformly charged molecule. There are some local inhomogeneities in its electrostatic profile which correlate with promoter sequences. Electrostatic patterns of promoter DNAs can be specified due to the presence of some distinctive motifs which differ for different promoter groups and may be involved as signal elements in differential recognition of various promoters by the enzyme. Some specific electrostatic elements which are responsible for modulating promoter activities due to ADP-ribosylation of RNA polymerase α-subunit were found in far upstream regions of T4 phage early promoters and E. coli ribosomal promoters.

scholarly journals Activation by NarL at the Escherichia coli ogt promoter

2020 ◽  
Vol 477 (15) ◽  
pp. 2807-2820
Author(s):  
Patcharawarin Ruanto ◽  
David L. Chismon ◽  
Joanne Hothersall ◽  
Rita E. Godfrey ◽  
David J. Lee ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Response Regulator ◽  
Direct Interaction ◽  
Α Subunit ◽  
E Coli ◽  
Terminal Domain ◽  
Dna Alkyltransferase ◽  
Promoter Dna ◽  
Transcript Initiation

The Escherichia coli NarX/NarL two-component response-regulator system regulates gene expression in response to nitrate ions and the NarL protein is a global transcription factor, which activates transcript initiation at many target promoters. One such target, the E. coli ogt promoter, which controls the expression of an O6-alkylguanine-DNA-alkyltransferase, is dependent on NarL binding to two DNA targets centred at positions −44.5 and −77.5 upstream from the transcript start. Here, we describe ogt promoter derivatives that can be activated solely by NarL binding either at position −44.5 or position −77.5. We show that NarL can also activate the ogt promoter when located at position −67.5. We present data to argue that NarL-dependent activation of transcript initiation at the ogt promoter results from a direct interaction between NarL and a determinant in the C-terminal domain of the RNA polymerase α subunit. Footprinting experiments show that, at the −44.5 promoter, NarL and the C-terminal domain of the RNA polymerase α subunit bind to opposite faces of promoter DNA, suggesting an unusual mechanism of transcription activation. Our work suggests new organisations for activator-dependent transcription at promoters and future applications for biotechnology.

Identification of a mutation within the structural gene for the a subunit of DNA-dependent RNA polymerase of E. coli

1976 ◽  
Vol 145 (1) ◽  
pp. 19-22 ◽  
Author(s):  
H. Fujiki ◽  
P. Palm ◽  
W. Zillig ◽  
R. Calendar ◽  
M. Sunshine
Keyword(s):  
Rna Polymerase ◽  
Structural Gene ◽  
E Coli ◽  
A Subunit

scholarly journals Transcriptional Activation of Agrobacterium tumefaciens Virulence Gene Promoters in Escherichia coli Requires the A. tumefaciens rpoA Gene, Encoding the Alpha Subunit of RNA Polymerase

1999 ◽  
Vol 181 (15) ◽  
pp. 4533-4539 ◽  
Author(s):  
S. M. Lohrke ◽  
S. Nechaev ◽  
H. Yang ◽  
K. Severinov ◽  
S. J. Jin
Keyword(s):  
Escherichia Coli ◽  
Agrobacterium Tumefaciens ◽  
Rna Polymerase ◽  
Virulence Genes ◽  
Virulence Gene ◽  
Dependent Manner ◽  
Gene Promoters ◽  
Gene Encoding ◽  
Α Subunit ◽  
E Coli

ABSTRACT The two-component regulatory system, composed of virAand virG, is indispensable for transcription of virulence genes within Agrobacterium tumefaciens. However,virA and virG are insufficient to activate transcription from virulence gene promoters within Escherichia coli cells, indicating a requirement for additional A. tumefaciens genes. In a search for these additional genes, we have identified the rpoA gene, encoding the α subunit of RNA polymerase (RNAP), which confers significant expression of avirB promoter (virBp)::lacZ fusion in E. coli in the presence of an active transcriptional regulatorvirG gene. We conducted in vitro transcription assays using either reconstituted E. coli RNAP or hybrid RNAP in which the α subunit was derived from A. tumefaciens. The two forms of RNAP were equally efficient in transcription from a ς70-dependent E. coli galP1 promoter; however, only the hybrid RNAP was able to transcribe virBpin a virG-dependent manner. In addition, we provide evidence that the α subunit from A. tumefaciens, but not from E. coli, is able to interact with the VirG protein. These data suggest that transcription of virulence genes requires specific interaction between VirG and the α subunit of A. tumefaciens and that the α subunit from E. coli is unable to effectively interact with the VirG protein. This work provides the basis for future studies designed to examinevir gene expression as well as the T-DNA transfer process in E. coli.

scholarly journals The RNA Polymerase α Subunit from Sinorhizobium meliloti Can Assemble with RNA Polymerase Subunits from Escherichia coli and Function in Basal and Activated Transcription both In Vivo and In Vitro

2002 ◽  
Vol 184 (14) ◽  
pp. 3808-3814 ◽  
Author(s):  
Melicent C. Peck ◽  
Tamas Gaal ◽  
Robert F. Fisher ◽  
Richard L. Gourse ◽  
Sharon R. Long
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Sinorhizobium Meliloti ◽  
Core Promoter ◽  
Temperature Sensitive ◽  
Protein Sequence Analysis ◽  
Α Subunit ◽  
E Coli

ABSTRACT Sinorhizobium meliloti, a gram-negative soil bacterium, forms a nitrogen-fixing symbiotic relationship with members of the legume family. To facilitate our studies of transcription in S. meliloti, we cloned and characterized the gene for the α subunit of RNA polymerase (RNAP). S. meliloti rpoA encodes a 336-amino-acid, 37-kDa protein. Sequence analysis of the region surrounding rpoA identified six open reading frames that are found in the conserved gene order secY (SecY)-adk (Adk)-rpsM (S13)-rpsK (S11)-rpoA (α)-rplQ (L17) found in the α-proteobacteria. In vivo, S. meliloti rpoA expressed in Escherichia coli complemented a temperature sensitive mutation in E. coli rpoA, demonstrating that S. meliloti α supports RNAP assembly, sequence-specific DNA binding, and interaction with transcriptional activators in the context of E. coli. In vitro, we reconstituted RNAP holoenzyme from S. meliloti α and E. coli β, β′, and σ subunits. Similar to E. coli RNAP, the hybrid RNAP supported transcription from an E. coli core promoter and responded to both upstream (UP) element- and Fis-dependent transcription activation. We obtained similar results using purified RNAP from S. meliloti. Our results demonstrate that S. meliloti α functions are conserved in heterologous host E. coli even though the two α subunits are only 51% identical. The ability to utilize E. coli as a heterologous system in which to study the regulation of S. meliloti genes could provide an important tool for our understanding and manipulation of these processes.

RNA polymerase: Preparation and structural analysis of helical polymers

1984 ◽  
Vol 42 ◽  
pp. 152-153
Author(s):  
E. Loren Buhle ◽  
Pamela Rew ◽  
Ueli Aebi
Keyword(s):  
Structural Analysis ◽  
Rna Polymerase ◽  
Molecular Level ◽  
X Ray Diffraction ◽  
Helical Polymers ◽  
X Ray ◽  
E Coli ◽  
The Past ◽  
Ordered Arrays ◽  
Low Ionic Strength

While DNA-dependent RNA polymerase represents one of the key enzymes involved in transcription and ultimately in gene expression in procaryotic and eucaryotic cells, little progress has been made towards elucidation of its 3-D structure at the molecular level over the past few years. This is mainly because to date no 3-D crystals suitable for X-ray diffraction analysis have been obtained with this rather large (MW ~500 kd) multi-subunit (α2ββ'ζ). As an alternative, we have been trying to form ordered arrays of RNA polymerase from E. coli suitable for structural analysis in the electron microscope combined with image processing. Here we report about helical polymers induced from holoenzyme (α2ββ'ζ) at low ionic strength with 5-7 mM MnCl2 (see Fig. 1a). The presence of the ζ-subunit (MW 86 kd) is required to form these polymers, since the core enzyme (α2ββ') does fail to assemble into such structures under these conditions.

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