title: Conformation and length of the signal sequence affect processing of secretory protein.
abstract: Processing of human lysozyme with artificially designed signal sequences was examined in an in vitro translation-translocation system and compared with their secretory capabilities in yeast. It has been shown that the conformation of the C-terminal region of the signal sequence and the length of the hydrophobic segment are important factors for efficient cleavage of the signal sequence.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Kohara
authors.forename: Y
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: M
authors.initials: M
authors.lastname: Kikuchi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002474:Cell-Free System; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009113:Muramidase / Q000096:biosynthesis / Q000235:genetics*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000737:chemistry* / Q000378:metabolism*; D011817:Rabbits; D011994:Recombinant Proteins / Q000096:biosynthesis; D012156:Reticulocytes / Q000378:metabolism; D014158:Transcription, Genetic; D014357:Trypsin
chemical_list: D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D009113:Muramidase; D014357:Trypsin