The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

  • Homologues
  • NCBI Gene
  • NCBI SNP
  • iHOP resource
  • SNPedia
  • UniProt

Table of contents

About

Terms

 

Gene Review: 

ALG6  -  dolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol...

Saccharomyces cerevisiae S288c

Synonyms: Asparagine-linked glycosylation protein 6, Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase, Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase, Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase, UNA544, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on ALG6

  • Microsomal membranes from a mutant strain that synthesized glucosylphosphodolichol but lacked the ability to transfer the glucosyl residue to the growing lipid-linked oligosaccharide (alg6) exhibited labeling with 5-azido[beta-32P]UDPGlc comparable to that found in microsomes from the wild-type strain [1].
  • These aberrant protein-linked oligosaccharides were processed by the addition of outer chain residues in the alg3, alg5, and alg6 mutants [2].
  • Monoglucosylated protein-linked oligosaccharides were detected in alg6 or alg5 mutant cells, which transfer Man9GlcNAc2 to protein; glucosylation was dependent on the inhibition of glucosidase II or the disruption of the gene encoding this enzyme [3].
  • Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway [4].
  • Alg6p has sequence similarity to Alg8p, a protein required for glucosylation of Glc1Man9GlcNAc2 [4].
 

Other interactions of ALG6

  • These mutants synthesize and transfer to nascent proteins truncated oligosaccharides lacking two (alg8) or three (alg5 and alg6) glucoses [5].

References

  1. Evidence that the synthesis of glucosylphosphodolichol in yeast involves a 35-kDa membrane protein. Palamarczyk, G., Drake, R., Haley, B., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  2. Yeast mutants deficient in protein glycosylation. Huffaker, T.C., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  3. Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence. Castro, O., Chen, L.Y., Parodi, A.J., Abeijón, C. Mol. Biol. Cell (1999) [Pubmed]
  4. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W., Aebi, M. Glycobiology (1996) [Pubmed]
  5. Glycosylation of yeast exoglucanase sequons in alg mutants deficient in the glucosylation steps of the lipid-linked oligosaccharide. Presence of glucotriose unit in Dol-PP-GlcNAc2Man9Glc3 influences both glycosylation efficiency and selection of N-linked sites. Muñoz, M.D., Hernández, L.M., Basco, R., Andaluz, E., Larriba, G. Biochim. Biophys. Acta (1994) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities