The interaction between tetracycline and the ar- chaeal elongation factor 1a from Sulfolobus solfa- taricus was investigated. The effects produced by this eubacterial antibiotic indicated that this inter- action involved the G-domain of the elongation factor 1a from S. solfataricus, although also the M- domain was required. In fact, in the presence of the antibiotic, an increase in the fluorescence quantum yield of the aromatic region was observed for elon- gation factor 1a from S. solfataricus and its trun- cated form lacking the C-terminal domain, but not for that lacking also the M-domain. The increase in quantum yield was restored when the G-domain of elongation factor 1a from S. solfataricus was fused to the M and the C-domains of the eubacterial ana- logue elongation factor Tu. Tetracycline inhibits protein synthesis catalysed by elongation factor 1a from S. solfataricus; this is accompanied by an increase in the GDP/GTP exchange rate and a slight inhibition of the intrinsic GTPase, suggesting that a main effect of the antibiotic was exerted on the GTP-bound form of the enzyme. Furthermore, the mixed inhibition observed for GTPase confirmed that the interaction, besides the G-domain, involved also other region(s) of elongation factor 1a from S. solfataricus. These results can be useful for studying potential side effects arising from the interaction between tetracycline and eukaryotic elongation factors.

Interaction Between the Antibiotic Tetracycline and the Elongation Factor 1 alpha from the Archaeon Sulfolobus solfataricus

MASULLO, Mariorosario
2011

Abstract

The interaction between tetracycline and the ar- chaeal elongation factor 1a from Sulfolobus solfa- taricus was investigated. The effects produced by this eubacterial antibiotic indicated that this inter- action involved the G-domain of the elongation factor 1a from S. solfataricus, although also the M- domain was required. In fact, in the presence of the antibiotic, an increase in the fluorescence quantum yield of the aromatic region was observed for elon- gation factor 1a from S. solfataricus and its trun- cated form lacking the C-terminal domain, but not for that lacking also the M-domain. The increase in quantum yield was restored when the G-domain of elongation factor 1a from S. solfataricus was fused to the M and the C-domains of the eubacterial ana- logue elongation factor Tu. Tetracycline inhibits protein synthesis catalysed by elongation factor 1a from S. solfataricus; this is accompanied by an increase in the GDP/GTP exchange rate and a slight inhibition of the intrinsic GTPase, suggesting that a main effect of the antibiotic was exerted on the GTP-bound form of the enzyme. Furthermore, the mixed inhibition observed for GTPase confirmed that the interaction, besides the G-domain, involved also other region(s) of elongation factor 1a from S. solfataricus. These results can be useful for studying potential side effects arising from the interaction between tetracycline and eukaryotic elongation factors.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11367/25552
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