Porphyrins and porphines inhibit the ribonuclease P reaction in vitro.
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.
Hori
Yoshiaki
Y
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan.
Bichenkova
Elena V
EV
Wilton
Amanda N
AN
Tanaka
Terumichi
T
Douglas
Kenneth T
KT
Kikuchi
Yo
Y
D004722:Endoribonucleases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D029968:Escherichia coli Proteins; D011166:Porphyrins / Q000737:chemistry / Q000494:pharmacology*; D016337:RNA, Catalytic / Q000037:antagonists & inhibitors* / Q000378:metabolism; D043262:Ribonuclease P
D004791:Enzyme Inhibitors; D029968:Escherichia coli Proteins; D011166:Porphyrins; D016337:RNA, Catalytic; C107018:porphine; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli