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

Shams‐Eldin, Hosam; Chaban, Bonnie; Niehus, Sebastian; Schwarz, Ralph Τ.; Jarrell, Ken F.

doi:10.1128/jb.01778-07

Cited by 34 publications

(50 citation statements)

References 25 publications

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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%

“…The initial works linking an N-glycan structure to the actions of specific gene products in Archaea were performed on M. voltae (71,(111)(112)(113). In the first of these studies, published mere days ahead of a similar study of Hfx.…”

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

“…Alg7 is known to catalyze the first committed step in the N-glycosylation pathway of eukaryotic cells, namely, the conversion of UDP-N-acetyl-D-glucosamine and DolP to UMP and DolPP-N-acetyl-D-glucosamine (66). AglH shares 25% identity and 41% similarity with S. cerevisiae Alg7 as well as motifs conserved in N-acetylglucosamine-1-phosphate (GlcNAc-1-P) transferase (GPT) proteins, including the motif believed to be the GPT active-site nucleophile region (VFVGDT in Alg7 and VFPGDT in AglH) (112,117). Efforts to show the direct involvement of AglH in the M. voltae N-linked glycosylation pathway proved unsuccessful, since all attempts to inactivate the encoding gene were unsuccessful (71).…”

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

“…Attempts to identify the first GT in the pathway, namely, the enzyme responsible for attachment of GlcNAc to the dolichol carrier, led to the identification of a gene (Mv1751), subsequently designated aglH (112). AglH is the only protein in the M. voltae genome that belongs to Pfam PF00953 (GT family 4), which also includes the eukaryotic enzyme N-acetylglucosamine-1-transferase (Alg7).…”

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

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N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

Jarrell

Ding

Meyer

et al. 2014

Microbiol Mol Biol Rev

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172

207

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SUMMARY N-glycosylation of proteins is one of the most prevalent posttranslational modifications in nature. Accordingly, a pathway with shared commonalities is found in all three domains of life. While excellent model systems have been developed for studying N-glycosylation in both Eukarya and Bacteria , an understanding of this process in Archaea was hampered until recently by a lack of effective molecular tools. However, within the last decade, impressive advances in the study of the archaeal version of this important pathway have been made for halophiles, methanogens, and thermoacidophiles, combining glycan structural information obtained by mass spectrometry with bioinformatic, genetic, biochemical, and enzymatic data. These studies reveal both features shared with the eukaryal and bacterial domains and novel archaeon-specific aspects. Unique features of N-glycosylation in Archaea include the presence of unusual dolichol lipid carriers, the use of a variety of linking sugars that connect the glycan to proteins, the presence of novel sugars as glycan constituents, the presence of two very different N-linked glycans attached to the same protein, and the ability to vary the N-glycan composition under different growth conditions. These advances are the focus of this review, with an emphasis on N-glycosylation pathways in Haloferax , Methanococcus , and Sulfolobus .

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Section: Pathway Of N-linked Glycosylation In Methanogenssupporting

confidence: 74%

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

See 3 more Smart Citations

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

Jarrell

Ding

Meyer

et al. 2014

Microbiol Mol Biol Rev

Self Cite

172

207

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N‐glycosylation in the thermoacidophilic archaeon Sulfolobus acidocaldarius involves a short dolichol pyrophosphate carrier

et al. 2016

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N-glycosylation is a post-translational modification that occurs across evolution. In the thermoacidophilic archaea Sulfolobus acidocaldarius, glycoproteins are modified by an N-linked tri-branched hexasaccharide reminiscent of the N-glycans assembled in Eukarya. Previously, hexose-bearing dolichol phosphate was detected in a S. acidocaldarius Bligh-Dyer lipid extract. Here, we used a specialized protocol for extracting lipid-linked oligosaccharides to detect a dolichol pyrophosphate bearing the intact hexasaccharide, as well as its biosynthetic intermediates. Furthermore, evidence for N-glycosylation of two S. acidocaldarius proteins by the same hexasaccharide and its derivatives was collected. These findings thus provide novel insight into archaeal N-glycosylation.

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Archaeal Flagella

VanDyke¹,

Ng²,

Chaban³

et al. 2008

Encyclopedia of Life Sciences

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The archaeal flagellum is a unique, ‘tail‐like’ structure used for motility by single‐celled organisms belonging to the domain Archaea. These intricate protein assemblies extend from the cell surface, rotating to generate thrust that propels the organism. Although archaeal flagella are functionally similar to the flagella found on bacteria, they differ significantly in structure and presumed mode of assembly. Key concepts The student will learn: Although functionally similar to bacterial flagella, archaeal flagella are unique motility structures in terms of their structure and assembly. The structure of the flagellum can be divided into three distinct components: the filament, hook and anchoring structure. Each of these components is constructed of specific proteins either encoded by genes residing within flagellar operons or of currently unknown genes. Assembly of the archaeal flagellum, which lacks the internal channel found in bacterial flagella, is thus believed to occur via incorporation of protein subunits at the base of the structure after they undergo the necessary posttranslational modifications of signal peptide cleavage and glycan addition. Archaea use this motility apparatus in combination with chemotaxis systems to bias their direction of movement towards environmental conditions more favourable for cell growth.

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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

Cited by 34 publications

References 25 publications

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

N‐glycosylation in the thermoacidophilic archaeon Sulfolobus acidocaldarius involves a short dolichol pyrophosphate carrier

Archaeal Flagella

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