Fluorescence quenching and kinetic studies of conformational changes induced by DNA and cAMP binding to cAMP receptor protein from Escherichia coli

Cyclic AMP receptor protein (CRP) regulates the expression of more then 100 genes in Escherichia coli. It is known that the allosteric activation of CRP by cAMP involves a long‐distance signal transmission from the N‐terminal cAMP‐binding domain to the C‐terminal domain of CRP responsible for the in...

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Veröffentlicht in:	The FEBS journal 2005-03, Vol.272 (5), p.1103-1116
Hauptverfasser:	Tworzydło, Magdalena, Polit, Agnieszka, Mikołajczak, Jan, Wasylewski, Zygmunt
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria Binding Sites cAMP receptor protein (CRP) CRP–DNA interactions Cyclic AMP - metabolism Cyclic AMP Receptor Protein - chemistry Cyclic AMP Receptor Protein - genetics Cyclic AMP Receptor Protein - metabolism Deoxyribonucleic acid DNA DNA, Bacterial - genetics DNA, Bacterial - metabolism Escherichia coli - metabolism fast kinetics Fluorescence fluorescence quenching FRET Gene expression Kinetics Mutagenesis Protein Binding Protein Conformation Proteins Signal transduction Tryptophan - chemistry Tryptophan - genetics
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