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Inhibition of eukaryotic ribonuclease P activity by aminoglycosides: kinetic studies
Author(s) -
Tekos Apostolos,
Tsagla Antigoni,
Stathopoulos Constantinos,
Drainas Denis
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02190-6
Subject(s) - aminoglycoside , kanamycin , neomycin , ribonuclease , tobramycin , rnase p , chemistry , dictyostelium discoideum , paromomycin , gentamicin , antibiotics , biochemistry , streptomycin , pharmacology , biology , rna , gene
The effect of several aminoglycoside antibiotics on ribonuclease P (RNase P) was investigated using an in vitro experimental system from Dictyostelium discoideum . Detailed kinetic analysis showed that all aminoglycosides tested (tobramycin, gentamicin, kanamycin, paromomycin, neomycin) behave as classical non‐competitive inhibitors, with neomycin being the strongest inhibitor. The inhibition effect is attributed to the electrostatic competition of the cationic aminoglycosides with magnesium ions required for catalysis. Increasing Mg 2+ ion concentrations reduced the effect of aminoglycosides on RNase P activity. Detailed kinetic analysis showed that aminoglycosides compete with Mg 2+ for common binding sites on RNase P holoenzyme.