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• W1970351628 endingPage "232" @default.
• W1970351628 startingPage "223" @default.
• W1970351628 abstract "Acetylcholinesterase from Torpedo californica (TcAChE) can be found as a glycosyl phosphatidylinositol (GPI)-anchored, membrane associated form. The C-terminal amino-acid sequence of the precursor protein resembles the signal peptide sequence found in proteins and enzymes destined for GPI-modification. Characteristics of such a signal peptide are a relatively polar stretch of amino acids, separating a cleavage- and modification-site (omega-site) residue from a hydrophobic C-terminus. We have introduced mutations, both at putative omega-sites and in the hydrophobic region, and analysed their effects on GPI-anchoring of TcAChE. Our results show that substitution of all three Ser residues in the region Ser542-Ser544 prevents GPI-modification and membrane anchoring. Individual substitution of each of these residues resulted in no or only a minor effect on the modification. We therefore conclude that more than one residue within this sequence can be utilised as the omega-site. Our analyses of double substitutions indicated that Ser543 and Ser544 are the preferred residues for GPI-modification. Moreover, the hydrophobic region is shown to be essential for GPI-anchoring of TcAChE." @default.
• W1970351628 created "2016-06-24" @default.
• W1970351628 creator A5030673388 @default.
• W1970351628 creator A5039892972 @default.
• W1970351628 date "1996-02-01" @default.
• W1970351628 modified "2023-09-27" @default.
• W1970351628 title "Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored form" @default.
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• W1970351628 doi "https://doi.org/10.1016/0167-4838(95)00205-7" @default.
• W1970351628 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8597567" @default.
• W1970351628 hasPublicationYear "1996" @default.
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