Difference between revisions of "YGL047W"

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'''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<ref name='S000080148'>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 {{SGDpaper|S000080148}} PMID 15615718</ref><ref name='S000086112'>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 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000086130'>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
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'''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<ref name='S000086130'>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 {{SGDpaper|S000086130}} PMID 16100113</ref><ref name='S000086112'>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 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000080148'>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
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  {{SGDpaper|S000080148}} PMID 15615718</ref>
 
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Revision as of 14:05, 16 January 2009

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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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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 Cite error: Closing </ref> missing for <ref> tag -->




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References

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  1. 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
  2. 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
  3. 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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References

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