The Kluyveromyces lactis α1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretory pathway

Abstract Mutants of Kluyveromyces lactis denominated vga (vanadate glycosylation affected) bear various combinations of glycosylation and cell-wall defects. The vga3 mutation of K. lactis was mapped in the KlOCH1 gene, encoding the functional homologue of the Saccharomyces cerevisiaeα1,6-mannosyltra...

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Bibliographic Details
Published in:FEMS yeast research 2006-05, Vol.6 (3), p.449-457
Main Authors: Uccelletti, Daniela, Farina, Francesca, Rufini, Silvia, Magnelli, Paula, Abeijon, Claudia, Palleschi, Claudio
Format: Article
Language:English
Subjects:
cell wall
Chitin
Glucans
Glycosylation
Kluyveromyces lactis
Mannoproteins
Mutants
OCH1
Vanadate
Yeast
β1,6‐glucan
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Summary:Abstract Mutants of Kluyveromyces lactis denominated vga (vanadate glycosylation affected) bear various combinations of glycosylation and cell-wall defects. The vga3 mutation of K. lactis was mapped in the KlOCH1 gene, encoding the functional homologue of the Saccharomyces cerevisiaeα1,6-mannosyltransferase. Quantitative analysis of cell-wall components indicated a noticeable increase of chitin and β1,6-glucans and a severe decrease of mannoproteins in the mutant cells as compared with the wild-type counterparts. Fine-structure determination of the β1,6-glucan polymer indicated that, in the vga3-1 strain, the β1,6-glucans are shorter and have more branches than in the wild-type strain. This suggests that cell-wall remodelling changes take place in K. lactis in the presence of glycosylation defects. Moreover, the vga3 cells showed a significantly improved capability of secreting heterologous proteins. Such a capability, accompanied by the highly reduced N-glycosylation, may be of biotechnological interest, especially when hyper-glycosylation of recombinant products must be avoided.
ISSN:1567-1356
1567-1364
DOI:10.1111/j.1567-1364.2006.00027.x