Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein

Mehtap Abu-Qarn, Assunta Giordano, Francesca Battaglia, Andrej Trauner, Paul G. Hitchen, Howard R. Morris, Anne Dell, Jerry Eichler

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

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.

Original languageEnglish
Pages (from-to)3140-3146
Number of pages7
JournalJournal of Bacteriology
Volume190
Issue number9
DOIs
StatePublished - 1 May 2008

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