Key result
Pentamidine inhibits the catalytic activity of the group I intron Ca.LSU by altering RNA folding, with complete inhibition achieved at 200 µM.
Pentamidine inhibits the catalytic activity of the group I intron Ca.LSU by binding to specific sites and altering RNA folding, likely by competing for magnesium binding sites.
Pentamidine's RNA-folding inhibition may merit preclinical antifungal testing; leaves open clinical relevance pending in vivo data.
The antimicrobial agent pentamidine inhibits the self-splicing of the group I intron Ca.LSU from the transcripts of the 26S rRNA gene of Candida albicans, but the mechanism of pentamidine inhibition is not clear. We show that preincubation of the ribozyme with pentamidine enhances the inhibitory effect of the drug and alters the folding of the ribozyme in a pattern varying with drug concentration. Pentamidine at 25 microM prevents formation of the catalytically active F band conformation of the precursor RNA and alters the ribonuclease T1 cleavage pattern of Ca.LSU RNA. The effects on cleavage suggest that pentamidine mainly binds to specific sites in or near asymmetric loops of helices P2 and P2.1 on the ribozyme, as well as to the tetraloop of P9.2 and the loosely paired helix P9, resulting in an altered structure of helix P7, which contains the active site. Positively charged molecules antagonize pentamidine inhibition of catalysis and relieve the drug effect on ribozyme folding, suggesting that pentamidine binds to a magnesium binding site(s) of the ribozyme to exert its inhibitory effect.
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Yi Zhang (2002) studied Candida albicans group I intron Ca.LSU. Pentamidine vs. Control (no pentamidine) was evaluated on Inhibition of self-splicing activity of Ca.LSU. Pentamidine inhibits the catalytic activity of the group I intron Ca.LSU by altering RNA folding, with complete inhibition achieved at 200 µM.
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