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