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Titolo:
FEM1, a Fusarium oxysporum glycoprotein that is covalently linked to the cell wall matrix and is conserved in filamentous fungi
Autore:
Schoffelmeer, EAM; Vossen, JH; van Doorn, AA; Cornelissen, BJC; Haring, MA;
Indirizzi:
Swammerdam Inst Life Sci, Sect Plant Pathol, NL-1098 SM Amsterdam, Netherlands Swammerdam Inst Life Sci Amsterdam Netherlands NL-1098 SM m, Netherlands
Titolo Testata:
MOLECULAR GENETICS AND GENOMICS
fascicolo: 1, volume: 265, anno: 2001,
pagine: 143 - 152
SICI:
1617-4615(200103)265:1<143:FAFOGT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; CANDIDA-ALBICANS; ALPHA-AGGLUTININ; MOLECULAR-CLONING; PROTEINS; YEAST; GENE; IDENTIFICATION; MANNOPROTEINS; MEMBRANE;
Keywords:
Fusarium oxysporum; hyphal cell wall; cell wall glycoprotein glycosylphosphatidylinositol (GPI) anchor protein secretion;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Vossen, JH Swammerdam Inst Life Sci, Sect Plant Pathol, Kruislaan 318, NL-1098 SM Amsterdam, Netherlands Swammerdam Inst Life Sci Kruislaan 318 Amsterdam Netherlands NL-1098 SM
Citazione:
E.A.M. Schoffelmeer et al., "FEM1, a Fusarium oxysporum glycoprotein that is covalently linked to the cell wall matrix and is conserved in filamentous fungi", MOL GENET G, 265(1), 2001, pp. 143-152

Abstract

As part of an investigation of the cell wall structure of plant pathogenic. filamentous fungi, we set out to characterize covalently bound cell wall glycoproteins (CWPs) of the tomato pathogen Fusarium oxysporum. N-terminal sequencing of an abundant 60-kDa CWP led to the cloning of the corresponding gene which we have designated FEM1 (Fusarium extracellular matrix protein). The gene contains an ORF encoding a primary translation product of 212 amino acids, including an N-terminal 17-amino acid secretion signal sequence. Furthermore, FEM1p contains two potential N-glycosylation sites, and is rich in serine and threonine residues (29%) that could serve as O-glycosyl addition sites. At its C-terminus the protein contains a 22-amino acid sequence with the characteristics of a glycosylphosphatidylinositol (GPI) anchoraddition signal. A mutant FEM1 protein lacking this GPI anchor addition signal is not retained in the fungal cell wall but released into the culture medium, indicating that in the wild-type protein this sequence functions toanchor the protein to the extracellular matrix. Southern analysis shows that FEM1 is present as a single-copy gene in all formae speciales of F. oxyporum tested and in F. solani. Database searches show that FEM1p homologous sequences are present in other filamentous fungi as well.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 11:35:52