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The Candida albicans CUG-decoding ser-tRNA has an atypical anticodon stem-loop structure.

V M Perreau¹, G Keith, W M Holmes

¹Research School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.

Journal of Molecular Biology

|November 5, 1999

Summary

In Candida species, a unique serine transfer RNA (tRNA) decodes the leucine CUG codon due to guanosine at position 33. This causes an unusual anticodon arm structure, reducing decoding ability and aiding species evolution.

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Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

In Candida species, the leucine CUG codon is decoded by a serine transfer RNA (tRNA). This tRNA possesses unusual characteristics, including a serine identity and a guanosine at position 33 (G33).

Purpose of the Study:

To investigate the structural and functional properties of the Candida albicans ser-tRNACAG that decodes the leucine CUG codon.
To determine the role of guanosine at position 33 (G33) in shaping the tRNA's structure and decoding ability.

Main Methods:

Enzymatic probing (V1 RNase, RnI nuclease) and chemical probing (Pb(2+), imidazole) of native Candida albicans ser-tRNACAG.
Analysis of in vitro transcripts with varying bases (G, C, U, A) at position 33.
Kinetics studies of G37 methylation using Escherichia coli m(1)G37 methyltransferase.

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Main Results:

The overall tertiary structure of the Candida albicans ser-tRNACAG resembles a typical serine tRNA, except for a disrupted anticodon stem.
A guanosine residue at position 33 specifically induces the atypical anticodon stem structure.
The G33-induced structural anomaly alters the kinetics of G37 methylation, indicating unusual anticodon arm conformation.

Conclusions:

The anticodon arm distortion in this novel tRNA, caused by G33, leads to reduced decoding efficiency.
This reduced decoding ability has allowed the evolution of this tRNA without causing species extinction.