2008
DOI: 10.1128/jb.01778-07
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Identification of the Archaeal alg7 Gene Homolog (Encoding N -Acetylglucosamine-1-Phosphate Transferase) of the N-Linked Glycosylation System by Cross-Domain Complementation in Saccharomyces cerevisiae

Abstract: The Mv1751 gene product is thought to catalyze the first step in the N-glycosylation pathway in Methanococcus voltae. Here, we show that a conditional lethal mutation in the alg7 gene (N-acetylglucosamine-1-phosphate transferase) in Saccharomyces cerevisiae was successfully complemented with Mv1751, highlighting a rare case of cross-domain complementation.

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Cited by 35 publications
(51 citation statements)
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“…Because of the many features that AglH shares with eukaryotic Alg7, it was proposed that the archaeal enzyme could serve as a functional homologue of Agl7. Experiments showed that M. voltae aglH was indeed able to complement a conditional lethal mutation in the alg7 gene of S. cerevisiae, demonstrating that AglH was a GlcNAc-1-P transferase and likely the GT that catalyzes the first step of the M. voltae N-glycosylation pathway (112). Very similar results were recently reported for S. acidocaldarius (118) (see below).…”
Section: Pathway Of N-linked Glycosylation In Methanogenssupporting
confidence: 74%
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“…Because of the many features that AglH shares with eukaryotic Alg7, it was proposed that the archaeal enzyme could serve as a functional homologue of Agl7. Experiments showed that M. voltae aglH was indeed able to complement a conditional lethal mutation in the alg7 gene of S. cerevisiae, demonstrating that AglH was a GlcNAc-1-P transferase and likely the GT that catalyzes the first step of the M. voltae N-glycosylation pathway (112). Very similar results were recently reported for S. acidocaldarius (118) (see below).…”
Section: Pathway Of N-linked Glycosylation In Methanogenssupporting
confidence: 74%
“…Further in vitro examination of the roles of AglH and AglK in the M. voltae N-glycosylation process revealed other interesting findings (110). The first of these concerned AglH, the GT proposed to act in the first step of the process (112). When AglH was overexpressed in E. coli and membranes from this strain served as the enzyme source, no transfer of GlcNAc from UDP-GlcNAc to either short (C 55 and C 60 ) or long (C 85 to C 105 ) DolP was observed, despite previous findings that aglH genes from both M. voltae and S. acidocaldarius were able to functionally complement a conditional lethal alg7 mutant of S. cerevisiae (112,118).…”
Section: Pathway Of N-linked Glycosylation In Methanogensmentioning
confidence: 99%
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