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Titolo:
Optimising the signal peptide for glycosyl phosphatidylinositol modification of human acetylcholinesterase using mutational analysis and peptide-quantitative structure-activity relationships
Autore:
Bucht, G; Wikstrom, P; Hjalmarsson, K;
Indirizzi:
Natl Def Res Estab, Dept Microbiol, S-90182 Umea, Sweden Natl Def Res Estab Umea Sweden S-90182 t Microbiol, S-90182 Umea, Sweden
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 2, volume: 1431, anno: 1999,
pagine: 471 - 482
SICI:
0167-4838(19990518)1431:2<471:OTSPFG>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE LIVER 5'-NUCLEOTIDASE; CEREVISIAE GAS1 PROTEIN; ANCHOR ATTACHMENT; ERYTHROCYTE ACETYLCHOLINESTERASE; SEQUENCE REQUIREMENTS; MEMBRANE-PROTEINS; C-TERMINUS; GLYCOSYLPHOSPHATIDYLINOSITOL; BIOSYNTHESIS; INHIBITION;
Keywords:
human acetylcholinesterase; glycosyl phosphatidylinositol anchoring; spacer region; omega+1 residue; omega+2 residue; peptide-quantitative structure-activity relationship;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Bucht, G Natl Def Res Estab, Dept Microbiol, Cementvagen 20, S-90182 Umea,Sweden Natl Def Res Estab Cementvagen 20 Umea Sweden S-90182 ea, Sweden
Citazione:
G. Bucht et al., "Optimising the signal peptide for glycosyl phosphatidylinositol modification of human acetylcholinesterase using mutational analysis and peptide-quantitative structure-activity relationships", BBA-PROT ST, 1431(2), 1999, pp. 471-482

Abstract

Glycosyl phosphatidylinositol (GPI)-modified proteins have a C-terminal signal peptide (GPIsp) that mediates the addition of a GPI-anchor to an aminoacid residue at the cleavage and modification site (omega-site). Within the GPIsp, a stretch of hydrophilic amino acid residues are found which constitutes the spacer region that separates the omega-site residue from a hydrophobic C-terminus. Deletions and insertions into the spacer region of humanacetylcholinesterase (AChE) show that the length of this spacer region is very important for efficient GPI-modification. Surprisingly, the natural length of the spacer region in human AChE was not optimal for the highest degree of GPI modification. The importance of the two adjacent residues downstream of the w-site, the omega+1 and omega+2 residues, was investigated by peptide-quantitative structure-activity relationships (Peptide-QSAR). A model was made that predicts the efficiency of the GPI modification when these residues are substituted with others, and suggests important features for these residues. The most preferred omega+1 and omega+2 residues, predicted by the model, in combination with an ideal spacer length resulted in an optimised GPIsp. This mutant protein is more efficiently GPI-modified than any mutant AChE tested thus far. (C) 1999 Elsevier Science B.V. All rights reserved.

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Documento generato il 14/07/20 alle ore 19:53:17