Amino-terminal presequence of the precursor of peroxisomal 3-ketoacyl-CoA thiolase is a cleavable signal peptide for peroxisomal targeting

doi:10.1016/0006-291X(91)92028-I

Biochemical and Biophysical Research Communications

Volume 181, Issue 3, 31 December 1991, Pages 947-954

https://doi.org/10.1016/0006-291X(91)92028-I Get rights and content

Abstract

To examine the function of the amino-terminal presequence of rat peroxisomal 3-ketoacyl-CoA thiolase precursor, fusion proteins of various amino-terminal regions of the precursor with non-peroxisomal enzymes were expressed in cultured mammalian cells. On immunofluorescence microscopy, all constructs carrying the presequence part exhibited punctate patterns of distribution, identical with that of catalase, a peroxisomal marker. Proteins lacking all or a part of the prepiece were found in the cytosol. These results indicate that the presequence of the thiolase has sufficient information for peroxisomal targeting.

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Citation Excerpt :
A second evolutionarily conserved PTS is found close to the amino-terminus of a subset of peroxisomal matrix proteins. This PTS2 was first described as a nonapeptide present in the amino-terminal cleavable presequence of rat peroxisomal thiolase [41–43]. Most PTS2s fit the following consensus -R-(LIVQ)-X-X-(LIVQH)-(LSGA)-X-(HQ)-(LA)- [43].
Peroxisomes are unique among the organelles of the endomembrane system. Unlike other organelles that derive most if not all of their proteins from the ER (endoplasmic reticulum), peroxisomes contain dedicated machineries for import of matrix proteins and insertion of membrane proteins. However, peroxisomes are also able to import a subset of their membrane proteins from the ER. One aspect of peroxisome biology that has remained ill defined is the role the various import pathways play in peroxisome maintenance. In this review, we discuss the available data on matrix and membrane protein import into peroxisomes.
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²: Present address: Virology Division, National Cancer Center Research Institute, Tsukiji, Chuo-ku, Tokyo 104, Japan.

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Amino-terminal presequence of the precursor of peroxisomal 3-ketoacyl-CoA thiolase is a cleavable signal peptide for peroxisomal targeting

Abstract

J. Biol. Chem

J. Biol. Chem

Gene

Gene

Annu. Rev. Cell Biol

J. Cell Biol

Mol. Cell. Biol

J. Cell Biol

BioEssays