Halobacterial glycoprotein biosynthesis

Sumper, Manfred

doi:10.1016/0304-4157(87)90005-0

Cited by 117 publications

(100 citation statements)

References 55 publications

(45 reference statements)

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“…The Halobacterium salinarum flagellin contains a sulfated glycoconjugate, N-linked through a glucose bridge and based on glucuronic or iduronic acid, similar to the glycan moiety found on the S-layer glycoprotein (420,468). More recently, Methanococcus voltae flagellins have been shown to contain a novel N-linked trisaccharide (453), despite the fact that earlier glycoprotein staining-based studies had failed to detect flagellar glycosylation in this species (195).…”

Section: Fig 1 Schematic Depiction Of the Glycosylation Of Thementioning

confidence: 93%

“…In contrast, tunicamycin has no effect on the biosynthesis of the Haloferax volcanii S-layer glycoprotein (99) and accordingly, the glycan moiety of the Haloferax volcanii S-layer glycoprotein does not include N-acetylglucosamine (242,280). Bacitracin is another drug that interferes with protein glycosylation via an interruption of the recycling of pyrophosphate-containing dolichol species (420). Accordingly, in Halobacterium salinarum, bacitracin interferes with the attachment of the repeating sulfated pentasaccharide found at the Asn-2 position of the Slayer glycoprotein (284,469), although not with the attachment of the sulfated polysaccharide found at the other N-glycosylation sites of the protein (469).…”

Section: Process Of Protein N-glycosylation In Archaeamentioning

confidence: 99%

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Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Fig 1 Schematic Depiction Of the Glycosylation Of Thementioning

confidence: 93%

Section: Process Of Protein N-glycosylation In Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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“…The presence of N-linked glycans on archaeal flagellins would be consistent with a type IV pilin-like assembly at the base of the structure and where the subunits cross the membrane prior to incorporation. Evidence has been presented in the halophiles that the transfer of the glycan to the flagellins does in fact occur on the periplasmic side of the membrane (10,32).…”

Section: Nano-lc-ms/ms Analysis Of Flagellin Peptidementioning

confidence: 99%

“…The flagellin of this organism has been shown to be glycosylated with N-linked sulfated oligosaccharides composed of glucose in 1,4 linkage to hexuronic acids (10,11). This post-translational modification is also found on purified S-layer protein from this organism.…”

mentioning

confidence: 99%

Identification and Characterization of the Unique N-Linked Glycan Common to the Flagellins and S-layer Glycoprotein of Methanococcus voltae

Voisin

Houliston

Kelly

et al. 2005

Journal of Biological Chemistry

130

144

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The flagellum of Methanococcus voltae is composed of four structural flagellin proteins FlaA, FlaB1, FlaB2, and FlaB3. These proteins possess a total of 15 potential N-linked sequons (NX(S/T)) and show a mass shift on an SDS-polyacrylamide gel indicating significant posttranslational modification. We describe here the structural characterization of the flagellin glycan from M. voltae using mass spectrometry to examine the proteolytic digests of the flagellin proteins in combination with NMR analysis of the purified glycan using a sensitive, cryogenically cooled probe. Nano-liquid chromatography-tandem mass spectrometry analysis of the proteolytic digests of the flagellin proteins revealed that they are post-translationally modified with a novel Nlinked trisaccharide of mass 779 Da that is composed of three sugar residues with masses of 318, 258, and 203 Da, respectively. In every instance the glycan is attached to the peptide through the asparagine residue of a typical N-linked sequon. The glycan modification has been observed on 14 of the 15 sequon sites present on the four flagellin structural proteins. The novel glycan structure elucidated by NMR analysis was shown to be a trisaccharide composed of ␤-ManpNAcA6Thr-(1-4)-␤-GlcpNAc3NAcA-(1-3)-␤-GlcpNAc linked to Asn. In addition, the same trisaccharide was identified on a tryptic peptide of the S-layer protein from this organism implicating a common N-linked glycosylation pathway.Glycosylation of prokaryotic proteins is now well accepted, and examples of N-and O-glycosylation and of attachment of glycosylphosphatidylinositol anchors can now be found in the literature (1, 2). However, in contrast to eukaryotic glycosylation systems, prokaryotic systems display considerable diversity in the structure of the respective glycans and the proximal monosaccharide linkage. As a consequence there is considerable interest in determining the structural and genetic basis of glycan production among these diverse prokaryotic systems.The archaeal flagellum is a unique motility structure that is distinct from the well characterized bacterial flagellum (3). In contrast to bacterial flagellar assembly where newly synthesized flagellin is incorporated at the distal tip of the filament, it is believed that mature archaeal flagellin is incorporated at the base of the filament. In recent studies, the assembly of archaeal flagellum has been shown to more closely resemble a second bacterial motility system, the type IV pilus, where the structural protein pilin is synthesized with an unusual signal peptide and a hydrophobic N terminus. In Archaea, signal peptidases have been shown to cleave a signal peptide of the preflagellin proteins to produce mature flagellin, which is then incorporated into the filament (4). Flagellated archaeal species have one to five flagellin genes organized into a fla locus (3). The marine archaeon Methanococcus voltae has four flagellin structural genes organized in two transcriptional units: one unit contains flaA, whereas the second unit contains flaB1, flaB...

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“…The notion that glycosylation is also widespread in prokaryotes is relatively recent (see reffor a review). In prokaryotic proteins glycosylation sites have only been localized in the flagellins and the cell surface glycoprotein of Halobacterium which belongs to the archaebacteriae [2] ; evidence for the existence of true glycoproteins among the bacteria is not beyond doubt 111 . We have recently reported the nucleotide sequence-derived amino-acid sequence of this S-layer protein which appeared to be extensively and heterogeneously glycosylated^.…”

mentioning

confidence: 99%

Evidence for Tyrosine-Linked Glycosaminoglycan in a Bacterial Surface Protein

Peters

Rudolf²,

Oschkinat³

et al. 1992

Biological Chemistry Hoppe-Seyler

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Summary:The S-layer protein of Acetogenium kivui was subjected to proteolysis with different proteases and several high molecular mass glycosaminoglycan peptides containing glucose, galactosamine and an unidentified sugar-related component were separated by molecular sieve chromatography and reversedphase HPLC and subjected to N-terminal sequence analysis. By methylation analysis glucose was found to be uniformly 1,6-linked, whereas galactosamine was exclusively 1,4-linked. Hydrazinolysis and subsequent amino-acid analysis as well as two-dimensional NMR spectroscopy were used to demonstrate that in these peptides carbohydrate was covalently linked to tyrosine. As all of the four Tyr-glycosylation sites were found to be preceded by valine, a new recognition sequence for glycosylation is suggested.

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Halobacterial glycoprotein biosynthesis

Cited by 117 publications

References 55 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Identification and Characterization of the Unique N-Linked Glycan Common to the Flagellins and S-layer Glycoprotein of Methanococcus voltae

Evidence for Tyrosine-Linked Glycosaminoglycan in a Bacterial Surface Protein

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