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Nucleic Acids Symposium Series 2002 2(1):111-112; doi:10.1093/nass/2.1.111
© 2002 by Oxford University Press
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Porphyrins and porphines inhibit the ribonuclease P reaction in vitro

Yoshiaki Hori1, Elena V. Bichenkova2, Amanda N. Wilton2, Terumichi Tanaka1, Kenneth T. Douglas2 and Yo Kikuchi1

1 Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan, 2 School of Pharmacy and Pharmaceutical Sciences, University of Manchester Manchester M13 9PL, U.K.

Porphyrin has been reported to bind to the T{Psi}C stem of tRNA. This site is also recognized by ribonuclease P, which is essential and ubiquitous endoribonuclease responsible for the maturation of 5' ends of tRNA precursors. Thus, we investigated the effects of porphyrins on the in vitro reaction of ribonuclease P from Escherichia coli. The results showed that some of porphyrins inhibited the reaction more strongly than any other inhibitors reported so far. In addition to the benzimidazole inhibition that we have previously reported, these unusual substrate-binding inhibitions may provide new leads for the novel anti-bacterial reagent design.


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