Activation of bacterial ribonuclease P by macrolides

作者：Toumpeki Chrisavgi; Vourekas Anastassios; Kalavrizioti Dimitra; Stamatopoulou Vassiliki; Drainas Denis^*

来源：Biochemistry, 2008, 47(13): 4112-4118.

DOI：10.1021/bi701488q

The effect of macrolide antibiotic spiramycin oh 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 pretRNA cleavage by E. coli RNase P holoenzyme and M1 RNA. The K-s and V-max, as well as the K-s(app) and Vmax(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 M I 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.

• 出版日期2008-4-1