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The peroxisomal targeting signal of 3‐oxoacyl‐coA thiolase from Saccharomyces cerevisiae

Ralf Erdmann

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Abstract

All peroxisomal 3-oxoacyl-CoA thiolases identified so far do not contain the previously identified tripeptide peroxisomal targeting signal at their carboxy-termini. For the two rat thiolases it was shown that their peroxisomal targeting signals are localized within the amino-terminal region of the proteins and are cleaved upon import. This report demonstrates that the N-terminal region of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae is essential for its peroxisomal targeting, and that the N-terminal 16 amino acids of yeast thiolase are sufficient to target the otherwise cytosolic small subunit of ribulose-1,5-bisphosphate carboxylase to peroxisomes for import.

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What this paper is about

All peroxisomal 3-oxoacyl-CoA thiolases identified so far do not contain the previously identified tripeptide peroxisomal targeting signal at their carboxy-termini. For the two rat thiolases it was shown that their peroxisomal targeting signals are localized within the amino-terminal region of the proteins and are cleaved upon import. This report demonstrates that the N-terminal region of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae is essential for its peroxisomal targeting, and that the N-terminal 16 amino acids of yeast thiolase are sufficient to target the otherwise cytosolic small subunit of ribulose-1,5-bisphosphate carboxylase to peroxisomes for import.

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OpenAlex reports 72 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

All peroxisomal 3-oxoacyl-CoA thiolases identified so far do not contain the previously identified tripeptide peroxisomal targeting signal at their carboxy-termini. For the two rat thiolases it was shown that their peroxisomal targeting signals are localized within the amino-terminal region of the proteins and are cleaved upon import. This report demonstrates that the N-terminal region of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae is essential for its peroxisomal targeting, and that the N-terminal 16 amino acids of yeast thiolase are sufficient to target the otherwise cytosolic small subunit of ribulose-1,5-bisphosphate carboxylase to peroxisomes for import.

Key concepts: Peroxisomal targeting signal, Peroxisome, Thiolase, Saccharomyces cerevisiae, Biology, Biochemistry, Yeast, Amino acid

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