Identification of AglE, a Second Glycosyltransferase Involved in N-Glycosylation of the Haloferax volcanii S-Layer Glycoprotein (Articolo in rivista)

Type
Label
  • Identification of AglE, a Second Glycosyltransferase Involved in N-Glycosylation of the Haloferax volcanii S-Layer Glycoprotein (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1128/JB.00056-08 (literal)
Alternative label
  • Abu-Qarn M; Giordano A; Battaglia F; Trauner A; Hitchen PG; Morris HR; Dell A; Eichler J (2008)
    Identification of AglE, a Second Glycosyltransferase Involved in N-Glycosylation of the Haloferax volcanii S-Layer Glycoprotein
    in Journal of bacteriology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Abu-Qarn M; Giordano A; Battaglia F; Trauner A; Hitchen PG; Morris HR; Dell A; Eichler J (literal)
Pagina inizio
  • 3140 (literal)
Pagina fine
  • 3146 (literal)
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  • 190 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 7 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 9 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel; Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, Pozzuoli (NA) 80078, Italy; Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom; M-SCAN, Ltd., Wokingham, Berks RG41 2TZ, United Kingdom (literal)
Titolo
  • Identification of AglE, a Second Glycosyltransferase Involved in N-Glycosylation of the Haloferax volcanii S-Layer Glycoprotein (literal)
Abstract
  • Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast to relatively advanced understanding of the eukaryal N glycosylation process and the information being amassed on the bacterial process, little is known of this posttranslational modification in Archaea. Toward remedying this situation, the present report continues ongoing efforts to identify components involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE, originally identified as a homologue of murine Dpm1, was shown to play a role in the addition of the 190-Da sugar subunit of the novel pentasaccharide decorating the S-layer glycoprotein. Topological analysis of an AglE-based chimeric reporter assigns AglE as an integral membrane protein, with its N-terminus and putative active site facing the cytoplasm. These finding, therefore, contribute to the developing picture of the N-glycosylation pathway in Archaea. (literal)
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