1887

Abstract

The structure and composition of the cell wall of yeast has so far been studied mainly in . It is basically made up of three components: -glucans, chitin and mannose-containing glycoproteins, also called mannoproteins. Most covalently bound cell-wall mannoproteins belong to the so-called glycosylphosphatidylinositol cell-wall protein (GPI-CWP) family, cell-wall proteins that are bound through the remnant of a GPI residue to 1,6--glucan. The non-conventional yeast shares Generally Regarded As Safe (GRAS) status with , has some industrial applications and is increasingly being proposed as a host for the production of recombinant proteins and as a model in the study of dimorphism. However, very little information on cell-wall structure and composition is available for this organism. Here is described the isolation and characterization of , a homologue of the gene from , which encodes a GPI-CWP, and the identification of its gene product. encodes a 221 aa protein that contains a putative signal peptide and a putative GPI-attachment site. It shows 28·5 % overall identity with Cwp1 of and a hydropathy profile characteristic of GPI-CWPs. Disruption of , both in the wild-type and in an glycosylation-deficient background, led to the identification of Ylcwp1 as a 60 kDa polypeptide present in cell-wall extracts. To the authors' knowledge, this is the first report of a GPI-CWP in , and it suggests that the cell-wall organization of is similar to that of .

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2004-01-01
2020-08-08
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