Targeting efficiencies of various permutations of the consensus C‐terminal tripeptide peroxisomal targeting signal

Abstract

Two types of peptide signals are known to independently target proteins into the peroxisomal matrix. One of these is a consensus C‐terminal tripeptide which is conserved in many microbody proteins derived from diverse species. The second signal is an N‐terminal sequence found in a small subset of peroxisomal proteins. We have tested 18 possible variants of the consensus tripeptide targeting signal for their ability to facilitate the transport of a cytosolic passenger protein, chloramphenicol acetyltransferase, into peroxisomes of monkey kidney cells. Our results reveal the presence of a hierarchy of preferred amino acid substitutions at each position of the tripeptide.