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J. Bacteriol. doi:10.1128/JB.00056-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

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

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, UK; M-SCAN Ltd., Wokingham, Berks RG41 2TZ, UK

^* To whom correspondence should be addressed. Email: jeichler{at}bgu.ac.il.

	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 post-translational modification in Archaea. Towards remedying this situation, the present report continues on-going 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.

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