Fate of highly expressed proteins destined to peroxisomes inSaccharomyces cerevisiae
✍ Scribed by A. Hartig; M. Ogris; G. Cohen; M. Binder
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 869 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0172-8083
No coin nor oath required. For personal study only.
✦ Synopsis
Import of proteins into organelles usually requires a cis-acting targeting signal. Analysis of various hybrid proteins, consisting of mouse DHFR and parts of catalase A from Saccharomyces cerevisiae, revealed that fusion proteins containing the N-terminal 126 amino acids, or less, of catalase A remain in the cytosol whereas fusion proteins containing 140, or more, N-terminal amino acids of catalase A form large aggregates inside the cell. These protein bodies, which lack a surrounding membrane, copurified with peroxisomes on cell fractionation. The peroxisomal targeting signal of catalase A does not reside at the C-terminus or at the N-terminus.