Rifampicin: an inhibitor of Xp12-specific protein phosphorylation in Xanthomonas oryzae pv. oryzae
1996
Cheng, C.M. | Tu, J. | Yang, C.C. | Kuo, T.T.
Phosphorylation of the three Xp12-specific phosphoproteins was drastically reduced by rifampicin, an antibiotic that specifically inhibits the host-cell RNA polymerase. However, this inhibitory effect could not be found in spontaneous mutants of Xanthomonas oryzae pv. oryzae whose RNA polymerase are resistant to the drug. The inhibitory effect of rifampicin treatment also resulted suppression of the Xp12 multiplication cycle. This implies the physiological significance of this effect and supports our previous prediction that phosphorylation plays an important role in the life cycle of Xp12. The acid- and alkali-labile character of the Xp12-specific phosphoproteins and the chemical stability of the phosphoryl linkages show that the corresponding protein kinase catalyzes the formation of an acyl phosphorylation. Subsequent fractionation of cell lysate revealed that the phosphoproteins were located in the periplasm. Actinomycin D, which affects transcription through DNA condensation rather than its binding to RNA polymerase, was not able to cause the inhibition effect. On the other hand, cerulenin was found to reduce the acyl phosphorylation which hints at a possible role of cell membrane in the phosphorylation. Here we present the evidence for the functional involvement of the rifampicin treatment on protein phosphorylation. A possible mechanism of rifampicin on the alternation of acyl phosphorylation is proposed.
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