Abstract
The firefly luciferase protein contains a peroxisomal targeting signal at its extreme COOH terminus (Gould et al., 1987). Site-directed mutagenesis of the luciferase gene reveals that this peroxisomal targeting signal consists of the COOH-terminal three amino acids of the protein, serine-lysine-leucine. When this tripeptide is appended to the COOH terminus of a cytosolic protein (chloramphenicol acetyltransferase), it is sufficient to direct the fusion protein into peroxisomes. Additional mutagenesis experiments reveal that only a limited number of conservative changes can be made in this tripeptide targeting signal without abolishing its activity. These results indicate that peroxisomal protein import, unlike other types of transmembrane translocation, is dependent upon a conserved amino acid sequence.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:18 p.m.) |
Deposited | 2 years, 1 month ago (July 21, 2023, 9 p.m.) |
Indexed | 3 weeks, 3 days ago (Aug. 5, 2025, 8:48 a.m.) |
Issued | 36 years, 3 months ago (May 1, 1989) |
Published | 36 years, 3 months ago (May 1, 1989) |
Published Online | 36 years, 3 months ago (May 1, 1989) |
Published Print | 36 years, 3 months ago (May 1, 1989) |
@article{Gould_1989, title={A conserved tripeptide sorts proteins to peroxisomes.}, volume={108}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.108.5.1657}, DOI={10.1083/jcb.108.5.1657}, number={5}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Gould, S J and Keller, G A and Hosken, N and Wilkinson, J and Subramani, S}, year={1989}, month=may, pages={1657–1664} }