Escherichia coli cAMP receptor protein: evidence for three protein conformational states with different promoter binding affinities

Biochemistry ◽  
1989 ◽  
Vol 28 (17) ◽  
pp. 6914-6924 ◽  
Author(s):  
Tomasz Heyduk ◽  
James C. Lee
Keyword(s):  
Escherichia Coli ◽  
Receptor Protein ◽  
Binding Affinities ◽  
Camp Receptor Protein ◽  
Conformational States ◽  
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

Determination of the rates of synthesis and degradation of adenosine 3′,5′-cyclic monophosphate in Escherichia coli CRP− and CRP+ strains

1978 ◽  
Vol 56 (9) ◽  
pp. 849-852 ◽  
Author(s):  
Ann D. E. Fraser ◽  
Hiroshi Yamazaki
Keyword(s):  
Escherichia Coli ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Balanced Growth ◽  
E Coli ◽  
Cyclic Monophosphate ◽  
Camp Receptor ◽  
Extracellular Camp ◽  
Synthesis And Degradation

We have developed a method for estimating the rates of synthesis and degradation of adenosine 3′,5′-cyclic monophosphate (cAMP) in Escherichia coli during balanced growth. Applying this method, we have found that an E. coli CRP− mutant 5333 (deficient for cAMP receptor protein) synthesizes cAMP about 25 times faster than does its CRP+ parent 1100. This accounts for the abnormally high intracellular and extracellular cAMP accumulation in 5333.

scholarly journals Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli

2008 ◽  
Vol 190 (13) ◽  
pp. 4532-4540 ◽  
Author(s):  
Hwan Youn ◽  
Junseock Koh ◽  
Gary P. Roberts
Keyword(s):  
Escherichia Coli ◽  
Binding Pocket ◽  
Receptor Protein ◽  
Ligand Specificity ◽  
Wild Type ◽  
Camp Receptor Protein ◽  
Active Protein ◽  
Common Basis ◽  
Affinity Ligand ◽  
Camp Receptor

ABSTRACT Activation of the cAMP receptor protein (CRP) from Escherichia coli is highly specific to its allosteric ligand, cAMP. Ligands such as adenosine and cGMP, which are structurally similar to cAMP, fail to activate wild-type CRP. However, several cAMP-independent CRP variants (termed CRP*) exist that can be further activated by both adenosine and cGMP, as well as by cAMP. This has remained a puzzle because the substitutions in many of these CRP* variants lie far from the cAMP-binding pocket (>10 Å) and therefore should not directly affect that pocket. Here we show a surprising similarity in the altered ligand specificity of four CRP* variants with a single substitution in D53S, G141K, A144T, or L148K, and we propose a common basis for this phenomenon. The increased active protein population caused by an equilibrium shift in these variants is hypothesized to preferentially stabilize ligand binding. This explanation is completely consistent with the cAMP specificity in the activation of wild-type CRP. The model also predicts that wild-type CRP should be activated even by the lower-affinity ligand, adenosine, which we experimentally confirmed. The study demonstrates that protein equilibrium is an integral factor for ligand specificity in an allosteric protein, in addition to the direct effects of ligand pocket residues.

Environmentally regulated algD promoter is responsive to the cAMP receptor protein in Escherichia coli

1991 ◽  
Vol 5 (10) ◽  
pp. 2503-2509 ◽  
Author(s):  
J. D. DeVault ◽  
W. Hendrickson ◽  
J. Kato ◽  
A. M. Chakrabarty
Keyword(s):  
Escherichia Coli ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Camp Receptor

Protection against nuclease cleavage of pBR322 DNA by the cAMP receptor protein of Escherichia coli

1983 ◽  
Vol 166 (1) ◽  
pp. 93-98 ◽  
Author(s):  
Angela M. Gronenborn ◽  
G. Marius Clore ◽  
Bruno Gronenborn ◽  
S. Brenner
Keyword(s):  
Escherichia Coli ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Pbr322 Dna ◽  
Camp Receptor
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