Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.

Yoshiaki Hori; Elena V. Bichenkova; Amanda N. Wilton; Terumichi Tanaka; Kenneth T. Douglas; Y. Kikuchi

Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.

Yoshiaki Hori, Elena V. Bichenkova, Amanda N. Wilton, Terumichi Tanaka, Kenneth T. Douglas, Y. Kikuchi

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract

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.

Original language	English
Title of host publication	Nucleic Acids Res Suppl\|Nucleic Acids Res Suppl
Pages	111-112
Number of pages	1
Publication status	Published - 2002

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@inproceedings{a1c45b98e45e40c3a87ee70bbad26e62,

title = "Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.",

abstract = "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.",

author = "Yoshiaki Hori and Bichenkova, {Elena V.} and Wilton, {Amanda N.} and Terumichi Tanaka and Douglas, {Kenneth T.} and Y. Kikuchi",

year = "2002",

language = "English",

pages = "111--112",

booktitle = "Nucleic Acids Res Suppl|Nucleic Acids Res Suppl",

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TY - GEN

T1 - Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.

AU - Hori, Yoshiaki

AU - Bichenkova, Elena V.

AU - Wilton, Amanda N.

AU - Tanaka, Terumichi

AU - Douglas, Kenneth T.

AU - Kikuchi, Y.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

M3 - Conference contribution

SP - 111

EP - 112

BT - Nucleic Acids Res Suppl|Nucleic Acids Res Suppl

ER -

Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.

Abstract

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