par Toumpeki, Chrisavgi;Vourekas, Anastassios;Kalavrizioti, Dimitra;Stamatopoulou, Vasiliki 
;Drainas, Denis
Référence Biochemistry, 47, 13, page (4112-4118)
Publication Publié, 2008-04
;Drainas, DenisRéférence Biochemistry, 47, 13, page (4112-4118)
Publication Publié, 2008-04
Article révisé par les pairs
| Résumé : | The effect of macrolide antibiotic spiramycin on RNase P holoenzyme and M1 RNA from Escherichia coli was investigated. Ribonuclease P (RNase P) is a ribozyme that is responsible for the maturation of 5' termini of tRNA molecules. Spiramycin revealed a dose-dependent activation on pre-tRNA cleavage by E. coli RNase P holoenzyme and M1 RNA. The K s and V max, as well as the K s(app) and V max(app) values of RNase P holoenzyme and M1 RNA in the presence or absence of spiramycin, were calculated from primary and secondary kinetic plots. It was found that the activity status of RNase P holoenzyme and M1 RNA is improved by the presence of spiramycin 18- and 12-fold, respectively. Primer extension analysis revealed that spiramycin induces a conformational change of the P10/11 structural element of M1 RNA, which is involved in substrate recognition. |
