| The Kluyveromyces lactis alpha1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretory pathway. | |
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MedLine Citation:
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PMID: 16630285 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Daniela Uccelletti; Francesca Farina; Silvia Rufini; Paula Magnelli; Claudia Abeijon; Claudio Palleschi |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: FEMS yeast research Volume: 6 ISSN: 1567-1356 ISO Abbreviation: FEMS Yeast Res. Publication Date: 2006 May |
Date Detail:
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Created Date: 2006-04-24 Completed Date: 2006-09-21 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 101085384 Medline TA: FEMS Yeast Res Country: Netherlands |
Other Details:
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Languages: eng Pagination: 449-57 Citation Subset: IM |
Affiliation:
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Department of Developmental and Cell Biology, University La Sapienza, Rome, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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GM 59773/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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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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