Novel fluorescent labelled affinity probes for diadenosine-5',5'''-P1,P4-tetraphosphate (Ap4A)-binding studies.
Tandem synthetic-biosynthetic procedures were used to prepare two novel fluorescent labelled affinity probes for diadenosine-5',5'''-P1,P4-tetraphosphate (Ap4A)-binding studies. These compounds (dial-mant-Ap4A and azido-mant-Ap4A) are shown to clearly distinguish known Ap4A-binding proteins from Escherichia coli (LysU and GroEL) and a variety of other control proteins. Successful labelling of chaperonin GroEL appears to be allosteric with respect to the well-characterized adenosine 5'-triphosphate (ATP)-binding site, suggesting that GroEL possesses a distinct Ap4A-binding site.
Wright
Michael
M
Imperial College Genetic Therapies Centre, Department of Chemistry, Flowers Building, Armstrong Road, Imperial College London, London SW7 2AZ, UK.
Miller
Andrew D
AD
D000495:Allosteric Site; D001665:Binding Sites; D001667:Binding, Competitive; D018834:Chaperonin 60 / Q000737:chemistry*; D015226:Dinucleoside Phosphates / Q000138:chemical synthesis / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000138:chemical synthesis / Q000737:chemistry*; D008968:Molecular Conformation
D018834:Chaperonin 60; D015226:Dinucleoside Phosphates; D005456:Fluorescent Dyes; C509745:azido-mant-Ap4A; C509744:dial-mant-Ap4A; C020733:diadenosine tetraphosphate