| Autor: |
Swinkels, Bart W., Gould, Stephen J., Subramani, Suresh |
| Zdroj: |
FEBS Letters; June 1992, Vol. 305 Issue: 2 p133-136, 4p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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