2 edition of study of transcription activation by the cyclic AMP receptor protein of Escherichia coli found in the catalog.
study of transcription activation by the cyclic AMP receptor protein of Escherichia coli
Roy Martin Williams
Thesis (Ph.D.) - University of Birmingham, School of Biochemistry.
|Statement||by Roy Martin Williams.|
1 Introduction. The cyclic AMP receptor protein (CRP, also known as CAP) of Escherichia coli is a transcription factor that regulates the expression of more than genes in the bacterium .It is a homodimer of ‐residue subunits, comprising the C‐terminal DNA binding domain (DBD, residues –) and the N‐terminal dimerisation domain that binds cAMP (CBD, residues . In Escherichia coli, cyclic AMP receptor protein (CRP) can regulate the transcription of more than genes. The signal to activate CRP is the binding of cyclic AMP. Binding of cAMP to CRP leads to a long-distance signal transduction from the N-terminal cAMP-binding domain to the C-terminal domain of the protein, which is responsible for.
In the course of a systematic screening of regulation targets of DNA-binding transcription factors from E. coli, we realized that CRP (cyclic AMP [cAMP] receptor protein), the global regulator for carbon source utilization, participates in regulation of some ribosomal protein genes, including the rmf gene. The CytR repressor antagonizes cyclic AMP-cyclic AMP receptor protein activation of the deoCp2 promoter of Escherichia coli K November Journal of Bacteriology (10)
activated by cyclic AMP receptor protein. J. Biol. Chem – Ebright RH, et al. Role of glutamic acid in DNA-sequence recognition by the catabolite gene activator protein (CAP) of Escherichia coli: altered DNA-sequence-recognition properties of [Val]CAP and [Leu]CAP. Proc. Natl. Acad. Sci. U. S. A. An ideal system to study allostery is the interaction of cyclic AMP (cAMP) and its receptor protein (CRP). cAMP and CRP are two “master elements” of a vast global regulatory network in Escherichia coli (reviewed in Kolb et al., ). The level of cAMP dramatically changes in response to the nature of energy sources for cell growth.
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The cyclic AMP receptor protein (CRP) activates transcription of the Escherichia coli acs gene, which encodes an acetate-scavenging enzyme required for fitness during periods of carbon starvation. Two promoters direct transcription of acs, the distal acs P1 and the proximal acs P2.
In this study, we demonstrated that acs P2 can function as the major promoter and showed by in vitro Cited by: 1. Introduction. The cyclic AMP receptor protein (CRP, also known as CAP) of Escherichia coli is a transcription factor that regulates the expression of more than genes in the bacterium.It is a homodimer of residue subunits, comprising the C-terminal DNA binding domain (DBD, residues –) and the N-terminal dimerisation domain that binds cAMP (CBD, Cited by: 6.
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The Escherichia coli paradigm. The cyclic-AMP receptor protein (CRP) and its effector cyclic-AMP (cAMP) were discovered in E. coli during investigations to explain the phenomenon of diauxic growth more than 40 years ago. Since then, E.
coli CRP–cAMP has become a paradigm of gene regulation, providing insights into signal perception and transduction, DNA recognition by regulatory proteins Cited by: Fluorescence polarization studies were used to study the interaction of a fluorescein-labelled conjugate of the Escherichia coli cyclic AMP receptor protein (F-CRP) and RNA polymerase.
Under conditions of physiological ionic strength, F-CRP binds to RNA polymerase holoenzyme in a cyclic AMP-dependent manner; the dissociation constant was about Cited by: In a previous study of promoters dependent on the Escherichia coli cyclic AMP receptor protein (CRP), carrying tandem DNA sites for CRP, we found that the upstream-bound CRP could either enhance or repress transcription, depending on its location.
Here, we have analyzed the interactions between CRP and the C-terminal domains of the RNA polymerase α subunits at some of these. Takahashi M, Blazy B, Baudras A. An equilibrium study of the cooperative binding of adenosine cyclic 3',5'-monophosphate and guanosine cyclic 3',5'-monophosphate to the adenosine cyclic 3',5'-monophosphate receptor protein from Escherichia coli.
Biochemistry. Oct 28; 19 (22)– Weber IT, Steitz TA. Semisynthetic promoters activated by Escherichia coli cyclic AMP receptor protein (CRP) were created by combining a synthetic CRP-binding site (crb) and nucleotide sequences derived from cryptic promoter regions.A bp oligodeoxyribonucleotide corresponding to an idealized crb was randomly placed into DNA regions that precede a promoterless lacZ gene on a plasmid.
Busby S, Ebright RH. Transcription activation by catabolite activator protein (CAP). J Mol Biol. Oct 22; (2)– Holcroft CC, Egan SM. Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon.
J Bacteriol. Transcription Activation Mediated by a Cyclic AMP Receptor Protein Escherichia coli CRP controls the activity of over genes and has been the most extensively studied so far (30, 72). This CRP was ﬁrst named the catabolite gene-activating protein, since it induces the transcription of a number of genes in.
TheCytRRepressorAntagonizes Cyclic AMP-CyclicAMPReceptor Protein Activation ofthe deoCp2Promoterof Escherichia coli K LOTTES0GAARD-ANDERSEN,JANMARTINUSSEN,NIELSERIKM0LLEGAARD,t STEPHENR.
DOUTHWAITE,ANDPOULVALENTIN-HANSEN* DepartmentofMolecularBiology, Odense University. Introduction. The cyclic AMP receptor protein (CRP) is a global transcription factor that plays a key role in controlling metabolism in enteric bacteria (Kolb et al., ; Barrett et al., ).CRP has been most studied in Escherichia coli K, and studies of individual gene-regulatory regions have suggested that its principal function is to activate transcription initiation at dozens of.
Transcription activation by cyclic AMP (cAMP) receptor protein (CAP) is the classic paradigm of transcription regulation in bacteria.
CAP was suggested to activate transcription on class-II. In Escherichia coli and related bacteria, cAMP controls gene expression (Botsford JL, ). This control occurs via the Catabolite gene Activator Protein (CAP, Zubay G, ), also called Cyclic AMP Receptor Protein (CRP, Emmer M, ), CRP at UniProtKB.
In E. coli, The CAP family of proteins includes FNR and YeiL. Reverse transcription-PCR showed that the fecA transcript was decreased in the Δ rpfF mutant compared to the wild type.
These data suggest that DSF affected the level of fecA mRNA. Transposon inactivation of crp, which encodes cyclic AMP (cAMP) receptor protein (CRP) resulted in reduced FecA expression and rpfF transcript level.
The Escherichia coli cyclic AMP receptor protein, CRP, induces transcription at Class II CRP-dependent promoters by making three different activatory contacts with different surfaces of holo RNA polymerase. One contact surface of CRP, known as Activating Region 3 (AR3), is functional in the downstream subunit of the CRP dimer and is predicted to interact with region 4 of the RNAP σ 70.
Protein-protein interactions during transcription activation: the case of the Escherichia coli cyclic AMP receptor protein. Savery N, Rhodius V, Busby S. Philos Trans R Soc Lond B Biol Sci, (), 01 Apr Cited by 16 articles | PMID: Review. Virgil A Rhodius, Stephen J.W Busby, Transcription activation by the Escherichia coli cyclic AMP receptor protein: determinants within activating region 3 1 1Edited by R.
Ebright, Journal of Molecular Biology, /jmbi,2, (), (). AMP (cAMP) receptor protein (CRP) protein. CRP is a well-studied global transcription regulator that binds to DNA as a dimer and activates transcription in the presence of cAMP. The activated Escherichia coli cAMP receptor protein, CRP, is capable of regulating the expression of more than 20 genes by binding to specific DNA sites.
DNA bending is an important structural feature that has been observed in the regulatory mechanism of gene expression by CRP. On the basis of the results of the fluorescence energy transfer study of the gal P1 promoter, gal bends. We have constructed a family of promoters carrying tandem DNA sites for the Escherichia coli cyclic AMP receptor protein (CRP), with one of the sites centred between base-pairs 41 and 42 upstream from the transcription start site, and the second site located further vivo activity measurements show that the activity of these promoters is completely dependent on CRP .Takahashi, T., Blazy, B., and Baudras, A.,An equilibrium study of the cooperative binding of adenosine cyclic 3’,5’-monophosphate and guanosine cyclic 3’,5’-monophosphate to the adenosine cyclic 3’,5’-monophosphate receptor protein from Escherichia coli, Biochemistry Abstract.
The 3′, 5′ cyclic adenoslne monophosphate (cAMP) binding pocket of the cAMP receptor protein (CRP) of Escheiichla coll was mutagenlzed to substitute leuclne, glutamine, or aspartate for glutamate 72; and lysine, histidine, leucine, Isoleuclne, or glutamine for arginine Substitutions were made In wild-type CRP and In a CRP *, or cAMP-lndependent, form of the protein to assess.