Reference : Crp of Streptomyces Coelicolor Is the Third Transcription Factor of the Large Crp-Fnr Su...
Scientific journals : Article
Life sciences : Biotechnology
Life sciences : Genetics & genetic processes
Life sciences : Microbiology
http://hdl.handle.net/2268/3514
Crp of Streptomyces Coelicolor Is the Third Transcription Factor of the Large Crp-Fnr Superfamily Able to Bind Camp
English
Derouaux, Adeline mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Dehareng, Dominique mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Lecocq, Elke [> > > >]
Halici, Serkan [> > > >]
Nothaft, Harald [> > > >]
Giannotta, Fabrizio [> > > >]
Moutzourelis, Georgios [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Dusart, Jean [Université de Liège - ULg > Services administratifs généraux > R&D : Gestion opérationnelle >]
Devreese, Bart [> > > >]
Titgemeyer, Fritz [> > > >]
Van Beeumen, Jozef [> > > >]
Rigali, Sébastien mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
17-Dec-2004
Biochemical and Biophysical Research Communications
325
3
983-90
Yes (verified by ORBi)
International
0006-291X
[en] cAMP-binding ability ; cAMP receptor protein ; germination-defective phenotype
[fr] streptomyces coelicolor
[en] The chromosomal inactivation of the unique transcription factor of Streptomyces coelicolor that displays a cyclic-nucleotide-binding domain, Crp(Sco), led to a germination-defective phenotype similar to the mutant of the adenylate cyclase gene (cya) unable to produce cAMP. By means of cAMP affinity chromatography we demonstrate the specific cAMP-binding ability of Crp(Sco), which definitely demonstrate that a Cya/cAMP/Crp system is used to trigger germination in S. coelicolor. However, electromobility shift assays with the purified Crp(Sco)-cAMP complex and the CRP-like cis-acting element of its own promoter failed. Moreover, we were unable to complement an Escherichia coli crp mutant in trans with Crp(Sco). The fact that Vfr from Pseudomonas aeruginosa and GlxR from Corynebacterium glutamicum could complement such an E. coli mutant suggests that the way Crp(Sco) interacts with DNA should mechanistically differ from its most similar members. This hypothesis was further supported by homology modelling of Crp(Sco) that confirmed an unusual organisation of the DNA-binding domain compared to the situation observed in Crp(Eco).
Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Fonds pour la formation à la Recherche dans l'Industrie et dans l'Agriculture (Communauté française de Belgique) - FRIA ; Deutsche Forschungsgemeinschaft - DFG
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/3514
10.1016/j.bbrc.2004.10.143

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