COOH-terminal requirements for the correct processing of a phosphatidylinositol-glycan anchored membrane protein.
作者： J Berger , A D Howard , L Brink , L Gerber , J Hauber
DOI: 10.1016/S0021-9258(19)81619-8
关键词: Membrane protein 、 Peptide sequence 、 Biochemistry 、 Chemistry 、 Translocon 、 Peptide 、 Wild type 、 COS cells 、 Complementary DNA 、 Mutant
摘要: Placental alkaline phosphatase (PLAP) is anchored to the plasma membrane by a phosphatidylinositol-glycan (PI-G) moiety. During processing of nascent PLAP, 29-residue COOH-terminal peptide cleaved out and PI-G moiety attached newly created COOH terminus mature protein. To investigate structural requirements protein for tailing anchoring membrane, we have transfected COS cells with wild type mutant forms cDNA encoding human prepro-PLAP. Utilizing series deletion mutants prepro-PLAP, it was found that be PI-G-tailed synthesized must possess an uncharged, predominantly hydrophobic amino acid sequence minimal length in peptide. While prepro-PLAP 17 consecutive residues terminal yielded membrane-bound products, 13 or fewer such hydrophilic proteins were no longer but efficiently secreted into medium. Studies using cassette demonstrated precise region could altered as long hydrophobicity maintained.
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