Document Detail


The Kluyveromyces lactis alpha1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretory pathway.
MedLine Citation:
PMID:  16630285     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 cerevisiaealpha1,6-mannosyltransferase. Quantitative analysis of cell-wall components indicated a noticeable increase of chitin and beta1,6-glucans and a severe decrease of mannoproteins in the mutant cells as compared with the wild-type counterparts. Fine-structure determination of the beta1,6-glucan polymer indicated that, in the vga3-1 strain, the beta1,6-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.
Authors:
Daniela Uccelletti; Francesca Farina; Silvia Rufini; Paula Magnelli; Claudia Abeijon; Claudio Palleschi
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEMS yeast research     Volume:  6     ISSN:  1567-1356     ISO Abbreviation:  FEMS Yeast Res.     Publication Date:  2006 May 
Date Detail:
Created Date:  2006-04-24     Completed Date:  2006-09-21     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  101085384     Medline TA:  FEMS Yeast Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  449-57     Citation Subset:  IM    
Affiliation:
Department of Developmental and Cell Biology, University La Sapienza, Rome, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Cell Wall / chemistry,  metabolism,  physiology*
Chitin / analysis
Fungal Proteins / chemistry,  genetics,  physiology
Gene Deletion
Genetic Complementation Test
Glycosylation
Kluyveromyces / enzymology*,  physiology
Mannosyltransferases / chemistry,  genetics,  physiology*
Membrane Glycoproteins / analysis
Molecular Sequence Data
Mutation
Protein Transport*
Sequence Homology, Amino Acid
beta-Glucans / analysis,  chemistry
Grant Support
ID/Acronym/Agency:
GM 59773/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Membrane Glycoproteins; 0/beta-Glucans; 0/mannoproteins; 1398-61-4/Chitin; EC 2.4.1.-/Mannosyltransferases; EC 2.4.1.-/alpha 1,6-mannosyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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