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Titolo:
Functional characterization of Gms1p/UDP-galactose transporter in Schizosaccharomyces pombe
Autore:
Tanaka, N; Takegawa, K;
Indirizzi:
Kagawa Univ, Fac Agr, Dept Life Sci, Miki, Kagawa 7610795, Japan Kagawa Univ Miki Kagawa Japan 7610795 fe Sci, Miki, Kagawa 7610795, Japan
Titolo Testata:
YEAST
fascicolo: 8, volume: 18, anno: 2001,
pagine: 745 - 757
SICI:
0749-503X(200106)18:8<745:FCOGTI>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
UDP-GALACTOSE TRANSPORTER; CMP-SIALIC ACID; N-ACETYLGLUCOSAMINE TRANSPORTER; NUCLEOTIDE-SUGAR TRANSPORTERS; GDP-MANNOSE TRANSPORTER; GOLGI-APPARATUS; FISSION YEAST; MOLECULAR-CLONING; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM;
Keywords:
UDP-galactose transporter; fission yeast; Golgi membrane; galactosylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Takegawa, K Kagawa Univ, Fac Agr, Dept Life Sci, Miki, Kagawa 7610795, Japan Kagawa Univ Miki Kagawa Japan 7610795 , Kagawa 7610795, Japan
Citazione:
N. Tanaka e K. Takegawa, "Functional characterization of Gms1p/UDP-galactose transporter in Schizosaccharomyces pombe", YEAST, 18(8), 2001, pp. 745-757

Abstract

Galactosylation of glycoproteins in the fission yeast Schizosaccharomyces pombe requires the transport of UDP-galactose as substrate for the galactosyltransferase into the lumen of the Golgi apparatus, which is achieved by the UDP-galactose transporter. We isolated a mutant (gms1) that is deficientin galactosylation of cell surface glycoproteins in Sr. pombe, and found that the gms1(+) gene encodes a UDP-galactose transporter. In the predictionof secondary structure of the Gms1 protein, an eight-membrane-spanning structure was obtained. Fluorescent microscopy revealed the functional Gms1-GFP fusion protein to be stably localized at the Golgi membrane. Sequencing analysis of the coding region of Gms1p derived from galactosylation-defective mutants identified a single amino acid mutation (A102T or A258E) located within the putative transmembrane region, helix 2 or helix 7, respectively. The mutagenized Gms1(A102T or A258E)p exhibited loss of UDP-galactose transport activity but no change in the localization to the Golgi membrane. TheC-terminal truncated Gms1p mutants demonstrated that the C-terminal hydrophilic region was dispensable for targeting and function as UDP-galactose transporter at the Golgi membrane. We suggest that the putative eighth (the most C-terminus-proximal) transmembrane helix of Gms1p is critical to targeting from ER to the Golgi membrane. Copyright (C) 2001 Jogn Wiley & Sons, Ltd.

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Documento generato il 01/12/20 alle ore 21:29:48