Difference between revisions of "YGL047W"
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| − | + | Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived. | |
| + | Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation. | ||
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==References== | ==References== | ||
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Revision as of 06:04, 14 May 2008
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| Systematic name | YGL047W |
| Gene name | ALG13 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VII:411555..412163 |
| Primary SGDID | S000003015 |
Description of YGL047W: Catalytic component of UDP-GlcNAc transferase, required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; similar to bacterial and human glycosyltransferases[1][2][3]
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Contents
Community Commentary
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Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived. Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation.
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References
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- ↑ Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6 SGD PMID 16100113
- ↑ Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 SGD PMID 16100110
- ↑ Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 SGD PMID 15615718
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