title: Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts.
abstract: Secretory signal peptides from individual prokaryotic and eukaryotic species have been analyzed, and the lengths and amino acid compositions of the positively charged amino-terminal region, the central hydrophobic region, and the carboxy-terminal cleavage-region have been compared. We find distinct differences between species in all three regions. Implications for protein secretion in foreign hosts are discussed.
authors.affiliation: Department of Molecular Biology, Karolinska Institute, Huddinge Hospital, Sweden.
authors.forename: G
authors.initials: G
authors.lastname: von Heijne
authors.forename: L
authors.initials: L
authors.lastname: Abrahmsén
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000235:genetics*; D004798:Enzymes / Q000235:genetics; D014644:Genetic Variation; D007256:Information Systems; D008969:Molecular Sequence Data; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D013210:Staphylococcus / Q000235:genetics*; D013291:Streptococcus / Q000235:genetics*; D013302:Streptomyces / Q000235:genetics*
chemical_list: D004798:Enzymes; D021382:Protein Sorting Signals