Abstract:
:Reactions involving removal and addition of glucose to N-glycans in the ER (endoplasmic reticulum) are performed in higher eukaryotes by glucosidases I and II and the UDP-glucose:glycoprotein glucosyltransferase respectively. Monoglucosylated N-glycan structures have been implicated in glycoprotein folding or ER quality control. Components of the system appear across a range of organisms; however, the precise combination differs between organisms. We have identified putative components of the system in the protozoal organism Trypanosoma brucei by local alignment searching. The function of one of these components, a glucosidase II alpha-subunit homologue, has been confirmed by phenotyping a null mutant, and an ectopic expression cell line. A combination of MS, methylation linkage analysis, exoglycosidase digestion and partial acetolysis have been used to characterize three novel N-glycan structures on the variant surface glycoprotein of the null mutant. On the basis of our results, we propose that two N-glycan precursors are available for transfer to variant surface glycoprotein (variant 221) in the ER of T. brucei; only one of these precursors is glucosylated after transfer.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Jones D,Mehlert A,Ferguson MAdoi
10.1042/BST0320766keywords:
subject
Has Abstractpub_date
2004-11-01 00:00:00pages
766-8issue
Pt 5eissn
0300-5127issn
1470-8752pii
BST0320766journal_volume
32pub_type
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journal_title:Biochemical Society transactions
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doi:10.1042/0300-5127:0290292
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journal_title:Biochemical Society transactions
pub_type: 杂志文章,评审
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更新日期:2001-08-01 00:00:00
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journal_title:Biochemical Society transactions
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doi:10.1042/BST20191046
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journal_title:Biochemical Society transactions
pub_type: 杂志文章
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更新日期:1984-12-01 00:00:00
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journal_title:Biochemical Society transactions
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doi:10.1042/BST0330213
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journal_title:Biochemical Society transactions
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更新日期:2010-08-01 00:00:00
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更新日期:2012-12-01 00:00:00
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