Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The carboxyl terminus of Dictyostelium discoideum protein 1I encodes a functional glycosyl-phosphatidylinositol signal sequence
Autore:
Stevens, BA; White, IJ; Hames, BD; Hooper, NM;
Indirizzi:
Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9JT S2 9JT, W Yorkshire, England
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 2, volume: 1511, anno: 2001,
pagine: 317 - 329
SICI:
0005-2736(20010402)1511:2<317:TCTODD>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANCHORED MEMBRANE-PROTEINS; CELL-SURFACE GLYCOPROTEIN; MOLD POLYSPHONDYLIUM-PALLIDUM; ACID-REQUIREMENTS ADJACENT; CLEAVAGE ATTACHMENT SITE; RENAL DIPEPTIDASE; ADHESION PROTEIN; DIRECTED MUTAGENESIS; PHOSPHOLIPID-ANCHOR; PARASITIC PROTOZOA;
Keywords:
cellular slime mold; glycosyl-phosphatidylinositol; membrane dipeptidase; phospholipase C; Dictyostelium discoideum;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Hooper, NM Univ Leeds, Sch Biochem & Mol Biol, Woodhouse Lane, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Woodhouse Lane Leeds W Yorkshire England LS2 9JT and
Citazione:
B.A. Stevens et al., "The carboxyl terminus of Dictyostelium discoideum protein 1I encodes a functional glycosyl-phosphatidylinositol signal sequence", BBA-BIOMEMB, 1511(2), 2001, pp. 317-329

Abstract

The 1I gene is expressed in the prespore cells of culminating Dictyostelium discoideum. The open reading frame of 1I cDNA encodes a protein of 155 amino acids with hydrophobic segments at both its NH2- and COOH-termini that are indicative of a glycosyl-phosphatidylinositol (GPI)-anchored protein. AhexaHis-tagged form of 1I expressed in D. discoideum cells appeared on Western blot analysis as a doublet of 27 and 24 kDa, with a minor polypeptide of 22 kDa. None of the polypeptides were released from the cell surface with bacterial phosphatidylinositol-specific phospholipase C, although all three were released upon nitrous acid treatment, indicating the presence of a phospholipase-resistant GPI anchor. Further evidence for the C-terminal sequence of 1I acting as a GPI attachment signal was obtained by replacing theGPI anchor signal sequence of porcine membrane dipeptidase with that from 1I. Two constructs of dipeptidase with the 1I GPI signal sequence were constructed, one of which included an additional six amino acids in the hydrophilic spacer. Both of the resultant constructs were targeted to the surface of COS cells and were GPI-anchored as shown by digestion with phospholipaseC. indicating that the Dictyostelium GPI signal sequence is functional in mammalian cells. Site-specific antibodies recognising epitopes either side of the expected GPI anchor attachment site were used to determine the site of GPI anchor attachment in the constructs. These parallel approaches show that the C-terminal signal sequence of 1I can direct the addition of a GPI anchor. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 21:54:27