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Species‐specific variation in signal peptide design Implications for protein secretion in foreign hosts
Author(s) -
von Heijne Gunnar,
Abrahmsèn Lars
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80579-4
Subject(s) - signal peptide , secretion , cleavage (geology) , amino acid , secretory protein , peptide , peptide sequence , variation (astronomy) , amino acid residue , biology , biochemistry , microbiology and biotechnology , chemistry , gene , paleontology , fracture (geology) , physics , astrophysics
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.

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