The peroxisomal targeting signal of 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae.
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.
Erdmann
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Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
D000101:Acetyl-CoA C-Acetyltransferase / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002458:Cell Fractionation; D015870:Gene Expression; D008830:Microbodies / Q000201:enzymology / Q000378:metabolism*; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000502:physiology*; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D017384:Sequence Deletion / Q000502:physiology
D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D000101:Acetyl-CoA C-Acetyltransferase; D012273:Ribulose-Bisphosphate Carboxylase