Activation of bacterial ribonuclease P by macrolides.
Biochemistry
; 47(13): 4112-8, 2008 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-18330998
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Macrolídeos
/
Ribonuclease P
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Escherichia coli
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article