Elicitins form a family of 10-kDa holoproteins secreted by various Phytophthora species. The large-scale purification of parasiticein, a novel elicitin secreted by P. parasitica, led to the determination of its sequence. We have compared the necrotic activities and the primary and secondary structur
Targeting of proteins into the eukaryotic secretory pathway: Signal peptide structure/function relationships
โ Scribed by Steven F. Nothwehr; Jeffrey I. Gordon
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 849 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
โฆ Synopsis
Much progress has been made in recent years regarding the mechanisms of targeting of secretory proteins to, and across, the endoplasmic reticulum (ER) membrane. Many of the cellular components involved in mediating translocation across this bilayer have been identified and characterized. Polypeptide domains of secretory proteins, termed signal peptides, have been shown to be necessary, and in most cases sufficient, for entry of preproteins into the lumen of the ER. These NH2terminal segments appear to serve multiple roles in targeting and translocation. The structural features which mediate their multiple functions are currently the subject of intense study.
๐ SIMILAR VOLUMES