Dose-dependent inhibition of ribonuclease P activity by anthralin.
The effect of five different anthralin concentrations on tRNA biogenesis was investigated employing the ribonuclease P (RNase P) of the slime mold Dictyostelium discoideum as an in vitro cell-free experimental system. RNase P is an ubiquitous and essential enzyme that endonucleolytically cleaves all tRNA precursors to produce the mature 5' end. Anthralin revealed a dose-dependent inhibition of RNase P activity indicating that this compound may have a direct effect on tRNA biogenesis. Taking into account that anthralin has no structural similarities to the substrate (pre-tRNA) of RNase P, it seems reasonable to suggest that this compound may bind to allosteric inhibition sites of the enzyme.
Drainas
D
D
Department of Biochemistry, University of Patras, Greece. Drainas@med.upatras.gr
Papadimou
E
E
Monastirli
A
A
Tsambaos
D
D
Merk
H F
HF
D000818:Animals; D000875:Anthralin / Q000494:pharmacology*; D000891:Anti-Infective Agents, Local / Q000494:pharmacology*; D002474:Cell-Free System; D004023:Dictyostelium / Q000187:drug effects / Q000201:enzymology; D004722:Endoribonucleases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D007700:Kinetics; D016337:RNA, Catalytic / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D012343:RNA, Transfer / Q000096:biosynthesis; D043262:Ribonuclease P; D012259:Ribonuclease, Pancreatic / Q000378:metabolism
D000891:Anti-Infective Agents, Local; D004791:Enzyme Inhibitors; D016337:RNA, Catalytic; D012343:RNA, Transfer; D004722:Endoribonucleases; D043262:Ribonuclease P; D012259:Ribonuclease, Pancreatic; D000875:Anthralin