Haloferax volcanii AglB and AglD are Involved in N-glycosylation of the S-layer Glycoprotein and Proper Assembly of the Surface Layer

Abu-Qarn, Mehtap; Yurist-Doutsch, Sophie; Giordano, Assunta; Trauner, Andrej; Morris, Howard R.; Hitchen, Paul G.; Medalia, Ohad; Dell, Anne; Eichler, Jerry

doi:10.1016/j.jmb.2007.10.042

Cited by 124 publications

(282 citation statements)

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“…The complicated pathway of LLO biosynthesis in H. volcanii has been studied by Eichler's group for the past decade. Taking advantage of the established gene knock-out method, the functions of the Agl (archaeal glycosylation) proteins, including AglB, were investigated in detail (15,16). In parallel, they performed the normal phase liquid chromatography-electrospray ionization tandem mass spectrometry (NPLC-ESI-MS/MS) analysis of total lipid extracts from cultured cells, to elucidate the chemical structures of the LLOs.…”

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confidence: 99%

“…Another possibility is that the LLOs with shorter oligosaccharides are precursors in the LLO biosynthesis or breakdown products generated during the lipid preparation. To demonstrate that the Dol-P type LLO was actually the oligosaccharide donor for the N-glycosylation in H. volcanii, the changes in the oligosaccharide structures caused by the deletions of the agl genes were monitored on the Dol-P carrier and the S-layer glycoprotein (9,15,16). Imperiali's group (22) provided direct biochemical evidence that the Dol-P-disaccharide indeed served as an oligosaccharide donor for the AglB from the methanogenic archaeon, M. voltae.…”

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confidence: 99%

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Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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The glycosylation of asparagine residues is the predominant protein modification in all three domains of life. An oligosaccharide chain is preassembled on a lipid-phospho carrier and transferred onto asparagine residues by the action of a membrane-bound enzyme, oligosaccharyltransferase. The oligosaccharide donor for the oligosaccharyl transfer reaction is dolichol-diphosphate-oligosaccharide in Eukaryota and polyprenol-diphosphate-oligosaccharide in Eubacteria. The donor in some archaeal species was reportedly dolichol-monophosphate-oligosaccharide. Thus, the difference in the number of phosphate groups aroused interest in whether the use of the dolichol-monophosphate type donors is widespread in the domain Archaea. Currently, all of the archaeal species with identified oligosaccharide donors have belonged to the phylum Euryarchaeota. Here, we analyzed the donor structures of two species belonging to the phylum Crenarchaeota, Pyrobaculum calidifontis and Sulfolobus solfataricus, in addition to two species from the Euryarchaeota, Pyrococcus furiosus and Archaeoglobus fulgidus. The electrospray ionization tandem mass spectrometry analyses confirmed that the two euryarchaeal oligosaccharide donors were the dolichol-monophosphate type and newly revealed that the two crenarchaeal oligosaccharide donors were the dolichol-diphosphate type. This novel finding is consistent with the hypothesis that the ancestor of Eukaryota is rooted within the TACK (Thaum-, Aig-, Cren-, and Korarchaeota) superphylum, which includes Crenarchaea. Our comprehensive study also revealed that one archaeal species could contain two distinct oligosaccharide donors for the oligosaccharyl transfer reaction. The A. fulgidus cells contained two oligosaccharide donors bearing oligosaccharide moieties with different backbone structures, and the S. solfataricus cells contained two oligosaccharide donors bearing stereochemically different dolichol chains.The glycosylation of asparagine residues is the predominant protein modification throughout all three domains of life (1-3). The oligosaccharides attached to asparagine residues in glycoproteins (N-glycan) affect various properties of the proteins, including folding, conformation, solubility, and antigenicity. Carbohydrate-binding proteins, such as lectins, recognize the N-glycans. Within the lumen of the endoplasmic reticulum in eukaryotic cells, the N-glycan functions as a quality control tag in the endoplasmic reticulum-associated degradation (4). The N-glycosylation occurs in the consensus motif (referred to as the sequon) represented by Asn-Xaa-Ser/Thr, where Xaa can be any residue except Pro. The formation of the N-glycosidic bond, between the monosaccharide residue at the reducing end of an oligosaccharide and the side chain amide group of the asparagine residues in proteins, is catalyzed by a membranebound enzyme, oligosaccharyltransferase (OST) 2 (3). The eukaryotic OST enzyme is a multisubunit protein complex. Among the eight different membrane subunit proteins, the catalytic subunit is a po...

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confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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“…Five glycosyltransferases named AglJ, AglG, AglI, AglE and AglD are sequentially involved in the transfer of five residues to the dolichol phosphate carrier directly or indirectly [3235]. Finally, the oligosaccharyltransferase AglB delivers the pentasaccharide to S-layer glycoprotein Asn residues [32,34].…”

Section: S-layer Proteinsmentioning

confidence: 99%

Cellular and organellar membrane-associated proteins in haloarchaea: Perspectives on the physiological significance and biotechnological applications

Cai

Zhao

Hou

et al. 2012

Sci. China Life Sci.

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Halophilic archaea (haloarchaea) inhabit hypersaline environments, tolerating extreme salinity, low oxygen and nutrient availability, and in some cases, high pH (soda lakes) and irradiation (saltern ponds). Membrane-associated proteins of haloarchaea, such as surface layer (S-layer) proteins, transporters, retinal proteins, and internal organellar membrane proteins including intracellular gas vesicle proteins and those associated with polyhydroxyalkanoate (PHA) granules, contribute greatly to their environmental adaptations. This review focuses on these haloarchaeal cellular and organellar membrane-associated proteins, and provides insight into their physiological significance and biotechnological potential.

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“…O-Glycosylation of this protein occurs through binding of glucosyl (132) galactose disaccharides to a C-terminal threonine cluster (13,14). Of the seven putative N-glycosidic sequons found within the S-layer glycoprotein, it was determined that Asn-13 and Asn-83 are modified by a pentasaccharide comprising two hexoses, two hexuronic acids, and a methyl ester of hexuronic acid (15,16). It was also determined that the sequon at Asn-370 is not modified (15).…”

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confidence: 99%

“…Of the seven putative N-glycosidic sequons found within the S-layer glycoprotein, it was determined that Asn-13 and Asn-83 are modified by a pentasaccharide comprising two hexoses, two hexuronic acids, and a methyl ester of hexuronic acid (15,16). It was also determined that the sequon at Asn-370 is not modified (15). The aforementioned pentasaccharide became a model to study the protein N-glycosylation process in Archaea (17), and it has also been found decorating H. volcanii flagellins (18).…”

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confidence: 99%

A Rhomboid Protease Gene Deletion Affects a Novel Oligosaccharide N-Linked to the S-layer Glycoprotein of Haloferax volcanii

Parente

Casabuono

Ferrari

et al. 2014

Journal of Biological Chemistry

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Background: Rhomboid proteases are ubiquitous, and their role in Archaea has not been explored. Results: We generated a rhomboid deletion mutant that displayed a glycosylation defect. Conclusion: Deletion of a rhomboid protease gene altered S-layer glycoprotein N-glycosylation. Significance: This work provides structural characterization of a novel oligosaccharide bound to H. volcanii S-layer glycoprotein and relates a rhomboid protease with the protein glycosylation process.

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Haloferax volcanii AglB and AglD are Involved in N-glycosylation of the S-layer Glycoprotein and Proper Assembly of the Surface Layer

Cited by 124 publications

References 42 publications

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Cellular and organellar membrane-associated proteins in haloarchaea: Perspectives on the physiological significance and biotechnological applications

A Rhomboid Protease Gene Deletion Affects a Novel Oligosaccharide N-Linked to the S-layer Glycoprotein of Haloferax volcanii

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