Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts.
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.
von Heijne
G
G
Department of Molecular Biology, Karolinska Institute, Huddinge Hospital, Sweden.
Abrahmsén
L
L
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*
D004798:Enzymes; D021382:Protein Sorting Signals