z-logo
open-access-imgOpen Access
Porphyrins and porphines inhibit the ribonuclease P reaction in vitro
Author(s) -
Yoshiki Hori,
Elena V. Bichenkova,
Alan N. Wilton,
Takashi Tanaka,
Kenneth T. Douglas,
Yo Kikuchi
Publication year - 2002
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/2.1.111
Subject(s) - in vitro , ribonuclease , chemistry , biochemistry , rna , gene
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom