Down regulation of cAMP production by cAMP receptor protein in Escherichia coli: an assessment of the contributions of transcriptional and posttranscriptional control of adenylate cyclase

1996 ◽  
Vol 253 (1-2) ◽  
pp. 198-204 ◽  
Author(s):  
T. Inada ◽  
H. Takahashi ◽  
T. Mizuno ◽  
H. Aiba
Keyword(s):  
Escherichia Coli ◽  
Adenylate Cyclase ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Camp Production ◽  
Down Regulation ◽  
Posttranscriptional Control ◽  
Camp Receptor

scholarly journals Interactions between the Escherichia coli cAMP receptor protein and the C-terminal domain of the α subunit of RNA polymerase at Class I promoters

1999 ◽  
Vol 337 (3) ◽  
pp. 415-423 ◽  
Author(s):  
Emma C. LAW ◽  
Nigel J. SAVERY ◽  
Stephen J. W. BUSBY
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Transcription Initiation ◽  
Class I ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Α Subunit ◽  
Terminal Domain ◽  
Up Elements ◽  
Camp Receptor

The Escherichia coli cAMP receptor protein (CRP) is a factor that activates transcription at over 100 target promoters. At Class I CRP-dependent promoters, CRP binds immediately upstream of RNA polymerase and activates transcription by making direct contacts with the C-terminal domain of the RNA polymerase α subunit (αCTD). Since αCTD is also known to interact with DNA sequence elements (known as UP elements), we have constructed a series of semi-synthetic Class I CRP-dependent promoters, carrying both a consensus DNA-binding site for CRP and a UP element at different positions. We previously showed that, at these promoters, the CRP–αCTD interaction and the CRP–UP element interaction contribute independently and additively to transcription initiation. In this study, we show that the two halves of the UP element can function independently, and that, in the presence of the UP element, the best location for the DNA site for CRP is position -69.5. This suggests that, at Class I CRP-dependent promoters where the DNA site for CRP is located at position -61.5, the two αCTDs of RNA polymerase are not optimally positioned. Two experiments to test this hypothesis are presented.

scholarly journals The cyclic AMP (cAMP)-cAMP receptor protein complex functions both as an activator and as a corepressor at the tsx-p2 promoter of Escherichia coli K-12.

1991 ◽  
Vol 173 (17) ◽  
pp. 5419-5430 ◽  
Author(s):  
P Gerlach ◽  
L Søgaard-Andersen ◽  
H Pedersen ◽  
J Martinussen ◽  
P Valentin-Hansen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Protein Complex ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Complex Functions ◽  
P2 Promoter ◽  
Camp Receptor ◽  
K 12

scholarly journals Structural Energy Landscapes and Plasticity of the Microstates of Apo Escherichia coli cAMP Receptor Protein

Biochemistry ◽  
2019 ◽  
Vol 59 (4) ◽  
pp. 460-470 ◽  
Author(s):  
Rati Chkheidze ◽  
Wilfredo Evangelista ◽  
Mark A. White ◽  
Y. Whitney Yin ◽  
J. Ching Lee
Keyword(s):  
Escherichia Coli ◽  
Receptor Protein ◽  
Energy Landscapes ◽  
Camp Receptor Protein ◽  
Camp Receptor
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