Corrections - Spatial relationship of the δ Subunit and the Rifampicin Binding Site in RNA Polymerase of Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (10) ◽  
pp. 2312-2312
Author(s):  
Cheng-Wen Wu ◽  
Lynwood Yarbrough ◽  
Felicia Wu ◽  
Zaharia Hillel
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Binding Site ◽  
Spatial Relationship ◽  
Relationship Of

Structure−Function Relationship of the Influenza Virus RNA Polymerase:  Primer-Binding Site on the PB1 Subunit†

Biochemistry ◽  
2004 ◽  
Vol 43 (19) ◽  
pp. 5882-5887 ◽  
Author(s):  
Dmitry M. Kolpashchikov ◽  
Ayae Honda ◽  
Akira Ishihama
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Structure Function ◽  
Binding Site ◽  
Primer Binding Site ◽  
Virus Rna ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Relationship Of

Evidence for a ppGpp-binding site on Escherichia coli RNA polymerase: proximity relationship with the rifampicin-binding domain

1995 ◽  
Vol 15 (2) ◽  
pp. 255-265 ◽  
Author(s):  
Padmalatha S. Reddy ◽  
Arvind Raghavan ◽  
Dipankar Chatterji
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Binding Site ◽  
Binding Domain

Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites

Biochemistry ◽  
1983 ◽  
Vol 22 (7) ◽  
pp. 1650-1656 ◽  
Author(s):  
Richard I. Christopherson ◽  
Elizabeth Heyde ◽  
John F. Morrison
Keyword(s):  
Escherichia Coli ◽  
Spatial Relationship ◽  
Chorismate Mutase ◽  
Prephenate Dehydrogenase ◽  
Relationship Of

scholarly journals Spacing requirements for interactions between the C-terminal domain of the α subunit of Escherichia coli RNA polymerase and the cAMP receptor protein

1998 ◽  
Vol 330 (1) ◽  
pp. 413-420 ◽  
Author(s):  
S. Georgina LLOYD ◽  
J. W. Stephen BUSBY ◽  
J. Nigel SAVERY
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Binding Site ◽  
Transcription Initiation ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Α Subunit ◽  
Synthetic Promoters ◽  
Terminal Domain ◽  
Camp Receptor

During transcription initiation at bacterial promoters, the C-terminal domain of the RNA polymerase α subunit (αCTD) can interact with DNA-sequence elements (known as UP elements) and with activator proteins. We have constructed a series of semi-synthetic promoters carrying both an UP element and a consensus DNA-binding site for the Escherichia coli cAMP receptor protein (CRP; a factor that activates transcription by making direct contacts with αCTD). At these promoters, the UP element was located at a variety of distances upstream of the CRP-binding site, which was fixed at position -41.5 bp upstream of the transcript start. At some positions, the UP element caused enhanced promoter activity whereas, at other positions, it had very little effect. In no case was the CRP-dependence of the promoter relieved. DNase I and hydroxyl-radical footprinting were used to study ternary RNA polymerase-CRP-promoter complexes formed at two of the most active of these promoters, and co-operativity between the binding of CRP and purified α subunits was studied. The footprints show that αCTD binds to the UP element as it is displaced upstream but that this displacement does not prevent αCTD from being contacted by CRP. Models to account for this are discussed.

A novel RNA polymerase binding site upstream of the galactose promoter in Escherichia coli exhibits promoter-like activity

2001 ◽  
Vol 268 (8) ◽  
pp. 2344-2350 ◽  
Author(s):  
Runa Sur ◽  
Dipanwita Debnath ◽  
Jayanta Mukhopadhyay ◽  
Pradeep Parrack
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Binding Site ◽  
Polymerase Binding

Structural studies on the active site of Escherichia coli RNA polymerase. 2. Geometrical relationship of the interacting substrates

Biochemistry ◽  
1990 ◽  
Vol 29 (25) ◽  
pp. 5994-6002 ◽  
Author(s):  
Richard B. Beal ◽  
Rajasekharan P. Pillai ◽  
Peter P. Chuknyisky ◽  
Abraham Levy ◽  
Edward Tarien ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Active Site ◽  
Structural Studies ◽  
Relationship Of ◽  
Geometrical Relationship
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