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tRNA(Phe) binds aminoglycoside antibiotics.

S R Kirk¹, Y Tor

¹Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0358, USA.

Bioorganic & Medicinal Chemistry

|October 26, 1999

Summary

Aminoglycoside antibiotics bind to transfer RNA (tRNA), stabilizing its structure and altering its conformation. These findings reveal new interactions between antibiotics and RNA, impacting retroviral replication.

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Aminoglycoside antibiotics interact with various RNA molecules, including those crucial for retroviral replication.
Understanding these interactions is key to developing new therapeutic strategies.

Purpose of the Study:

To investigate the binding of neomycin B, kanamycin A, and Neo-Neo to yeast transfer RNA (tRNA(Phe)).
To determine the impact of aminoglycosides on tRNA(Phe) structure and function.

Main Methods:

Thermal denaturation studies
Fluorescence spectroscopy
Pb2+-mediated tRNA(Phe) cleavage assays
Gel mobility shift assays
Enzymatic and chemical footprinting

Main Results:

Aminoglycosides significantly stabilize tRNA(Phe) secondary and tertiary structures.
Neo-Neo, neomycin B, and kanamycin A exhibit varying degrees of inhibition on tRNA(Phe) cleavage.
Footprinting data identify the anticodon stem and loop junctions as preferred binding sites.

Conclusions:

Aminoglycosides interact with yeast tRNA(Phe), inducing conformational changes and stabilizing its structure.
The binding affinity varies among different aminoglycosides, with Neo-Neo showing the strongest effect.
Identified binding sites provide insights into the mechanism of aminoglycoside-RNA interactions.

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