Targeting efficiencies of various permutations of the consensus C-terminal tripeptide peroxisomal targeting signal.
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.
Swinkels
B W
BW
Department of Biology, University of California, San Diego La Jolla 92093-0322.
Gould
S J
SJ
Subramani
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D015500:Chloramphenicol O-Acetyltransferase / Q000235:genetics / Q000378:metabolism; D016384:Consensus Sequence; D004252:DNA Mutational Analysis; D005455:Fluorescent Antibody Technique; D000882:Haplorhini; D008830:Microbodies / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D010446:Peptide Fragments; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D015500:Chloramphenicol O-Acetyltransferase