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Mitochondrial ribosomal protein L32 (MrpL32) of Saccharomyces cerevisiae is homologous to the bacterial L32 ribosomal protein. MrpL32 carries an N-terminal mitochondrion-targeting sequence (MTS) and is about 60 amino acid residues longer at the C-terminus. Adding to its function as a leader sequence, the MTS of MrpL32 has been reported to regulate ribosome biogenesis through its processing by m-AAA protease. However, the function of the C-terminal extension (CE) remains totally unknown. Therefore, we constructed a series of C-terminally truncated mrpl32 (mrpl32ΔC) genes and expressed them in a Δmrpl32 mutant to examine their function. Interestingly, some MrpL32ΔC derivatives exhibited temperature-sensitive (ts) growth on medium with non-fermentable carbon sources. Furthermore, the CE domain of MrpL32, expressed separately from MrpL32ΔC, could rescue the ts phenotype of mutants by improving mitochondrial protein synthesis.

genes and genetic systems

The C-terminal extension domain of &lt;i&gt;Saccharomyces cerevisiae&lt;/i&gt; MrpL32, a homolog of ribosomal protein L32, functions &lt;i&gt;in&lt;/i&gt; &lt;i&gt;trans&lt;/i&gt; to support mitochondrial translation