The hydrophobic domains in the carboxyl-terminal signal for GPI modification and in the amino-terminal leader peptide have similar structural requirements

Journal of Molecular Biology
W YanM Ratnam

Abstract

Proteins having a glycosyl-phosphatidylinositol (GPI) membrane anchor are synthesized with a carboxyl-terminal signal that is cleaved in the endoplasmic reticulum prior to GPI modification. The signal is characterized by a moderately hydrophobic domain downstream from the cleavage/modification site. The essential features of this domain were characterized using a truncated version of folate receptor (FR) type beta (FR-beta delta 5) in which its five carboxyl-terminal amino acid residues were deleted without affecting the efficiency of GPI modification. The amino acids at various positions in the hydrophobic domain were systematically altered and the extent of GPI modification of the recombinant proteins was determined by measuring [3H]folic acid binding at the cell surface, by Western blot analysis and from the sensitivity of the proteins to phosphatidylinositol-specific phospholipase C (PI-PLC). The results indicate that a threshold level of hydrophobicity exists at a single position below which the efficiency of GPI modification decreases with increasing hydrophilicity. Further, the hydrophobic domain is characterized by a hydrophobicity profile and not merely a minimum overall hydrophobicity. Thus, a leucine-rich core hydrop...Continue Reading

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Citations

Dec 6, 2012·Chinese Journal of Integrative Medicine·Ana Paula de Sousa Fragoso, Arthur de Sá Ferreira
Aug 6, 2011·The Journal of Clinical Endocrinology and Metabolism·Sybil CharrièreChristophe Marçais
Jun 8, 2002·The Journal of Biological Chemistry·Saulius VainauskasAnant K Menon
Sep 25, 1999·Journal of Molecular Biology·B EisenhaberF Eisenhaber
Oct 15, 2009·Fungal Genetics and Biology : FG & B·Juliana T MaricatoJosé D Lopes

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