Cyclic nucleotide binding to cAMP receptor protein from Escherichia coli
- 1 November 1987
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 168 (3) , 687-694
- https://doi.org/10.1111/j.1432-1033.1987.tb13470.x
Abstract
CAMP receptor protein from Escherichia coli has been purified on a large scale. Analogues of cAMP modified on the 6‐NH2 group of the adenosine ring, the ribose 2′OH group or the cyclic phosphate are able to displace cAMP from its binding site with dissociation constants of similar magnitude to that of cAMP. More extensive modification produces weaker binding. Ultraviolet/visible difference spectroscopy and fluorescence spectroscopy show that the environment of the bound adenosine moiety is considerably less polar than that in aqueous solvent, while an anthraniloyl group substituted on the 2′OH position remains accessible to solvent. The 2‐NH2 group of cGMP appears to be protonated in the bound form, while no change in the charge state of cAMP is apparent.This publication has 31 references indexed in Scilit:
- Analogs of cyclic AMP that elicit the biochemically defined conformational change in catabolite gene activator protein (CAP) but do not stimulate binding to DNAJournal of Molecular Biology, 1985
- Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own geneCell, 1983
- Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine cyclic 3',5'-phosphate receptor proteinBiochemistry, 1982
- How cyclic AMP and its receptor protein act in escherichia coliCell, 1982
- 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 coliBiochemistry, 1980
- Ligand-induced change in the radius of gyration of cAMP receptor protein from Escherichia coliFEBS Letters, 1980
- A rapid high-yield purification procedure for the cyclic adenosine 3′,5′-monophosphate receptor protein from Escherichia coliBiochimica et Biophysica Acta (BBA) - General Subjects, 1978
- Cyclic AMP-mediated intersubunit disulfide crosslinking of the cyclic AMP receptor protein of Escherichia coliJournal of Molecular Biology, 1977
- Specific binding of CAP factor to lac promoter DNANature, 1975
- Conformational transitions of cyclic adenosine monophosphate receptor protein of Escherichia coli. Fluorescent probe studyBiochemistry, 1974