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FEBS Lett. 1992 Jun 29;305(2):133-6.

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

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Department of Biology, University of California, San Diego La Jolla 92093-0322.


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.

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