PMID: 2510820Aug 22, 1989Paper

Conformation and reactivity changes induced by N-methylkirromycin (aurodox) in elongation factor Tu

Biochemistry
C BalestrieriG Chinali

Abstract

Kirromycin and related antibiotics inhibit protein synthesis in bacteria by acting on elongation factor Tu (EF-Tu). We have studied the effects of N-methylkirromycin (aurodox) on some molecular properties of this protein. The binding of the antibiotic causes a dramatic variation in the protein fluorescence emission spectrum with the appearance of a new maximum at around 340 nm. Addition of aurodox to trypsinized EF-Tu resulted in an emission spectrum similar to that of the denatured intact factor. Fluorescence lifetime analysis performed by a multifrequency phase fluorometer indicated that the fluorescence emission of the factor is heterogeneous with the major component having a lifetime near 4.8 ns in the absence and 6.6 ns in the presence of the antibiotic. These results were interpreted in terms of an antibiotic-induced environmental modification of the unique tryptophan residue of the protein leading to an increase in its quantum yield. However, aurodox did not modify the solvent exposure of this residue, as judged by fluorescence quenching experiments. Moreover, 1-anilino-8-naphthalenesulfonate (ANS) binding studies, as well as analysis of the protein reactivity toward the sulfhydryl group reagent 5,5'-dithiobis(2-nitroben...Continue Reading

References

May 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·A ParmeggianiR Cortese
Dec 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·H WolfA Parmeggiani
Jan 1, 1973·The Journal of Antibiotics·J BergerE Grunberg
Jul 1, 1980·European Journal of Biochemistry·A WittinghoferR Leberman
Mar 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·K AraiM Wade

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