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Targeting efficiencies of various permutations of the consensus C‐terminal tripeptide peroxisomal targeting signal
Author(s) -
Swinkels Bart W.,
Gould Stephen J.,
Subramani Suresh
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80880-p
Subject(s) - peroxisomal targeting signal , tripeptide , peroxisome , protein targeting , signal peptide , chloramphenicol acetyltransferase , biochemistry , peptide sequence , amino acid , biology , microbiology and biotechnology , chemistry , membrane protein , gene , reporter gene , gene expression , membrane
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.