Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
LOCALIZATION OF AN ALPHA-1,2-GALACTOSYLTRANSFERASE ACTIVITY TO THE GOLGI-APPARATUS OF SCHIZOSACCHAROMYCES-POMBE
Autore:
CHAPPELL TG; HAJIBAGHERI MAN; AYSCOUGH K; PIERCE M; WARREN G;
Indirizzi:
UNIV LONDON UNIV COLL,MRC,MOLEC CELL BIOL LAB LONDON WC1E 6BT ENGLAND IMPERIAL CANC RES FUND LONDON WC2A 3PX ENGLAND DUKE UNIV,MED CTR,DEPT CELL BIOL DURHAM NC 27710
Titolo Testata:
Molecular biology of the cell
fascicolo: 5, volume: 5, anno: 1994,
pagine: 519 - 528
SICI:
1059-1524(1994)5:5<519:LOAAAT>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
FISSION YEAST; ACID-PHOSPHATASE; GLYCOSYLATION; PROTEIN; GENE; PATTERN; CLONING; SEARCH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
T.G. Chappell et al., "LOCALIZATION OF AN ALPHA-1,2-GALACTOSYLTRANSFERASE ACTIVITY TO THE GOLGI-APPARATUS OF SCHIZOSACCHAROMYCES-POMBE", Molecular biology of the cell, 5(5), 1994, pp. 519-528

Abstract

We have cloned a gene encoding an alpha 1,2 galactosyltransferase activity from Schizosaccharomyces pombe. The open reading frame of the gene (gma12 for galactomannan, alpha 1,2), combined with the previous protein purification (Chappell and Warren, 1989), predicts an O-linked glycoprotein with type II transmembrane topology. By homologous gene disruption, we have demonstrated that the gma12 gene product (gma12p) isnonessential. The deletion strain (gma12-D10::ura4) has a significantly reduced level of galactosyltransferase activity relative to the parental strain, but both in situ lectin binding and in vitro biochemicalassays demonstrate the presence of further galactosyltransferase activity in addition to gma12p. Although gma12p is not the only galactosyltransferase in S. pombe, it produces a unique carbohydrate structure on the surface of the yeast cells. We have generated a polyclonal antiserum against this carbohydrate epitope and shown that gma12p is capable of synthesizing the epitope both in vitro and in vivo. Electron microscopic localization of the gma12(+) specific epitope in gma12(+) cells revealed that gma12p synthesizes the carbohydrate structure in the Golgi apparatus, and subsequent intracellular transport distributes theepitope to later stages of the secretory pathway. The immunolocalization studies confirm the presence of one or more galactosyltransferase activities in the Golgi apparatus in fission yeast.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 11:07:32