Identification of AgIE, a Second Glycosyltransferase Involved in N Glycosylation of the Haloferax volcanii S-Layer Glycoprotein

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 i...

Full description

Saved in:
Bibliographic Details
Published inJournal of bacteriology Vol. 190; no. 9; p. 3140
Main Authors Abu-Qarn, Mehtap, Giordano, Assunta, Battaglia, Francesca, Trauner, Andrej, Hitchen, Paul G, Morris, Howard R, Dell, Anne, Eichler, Jerry
Format Journal Article
LanguageEnglish
Published Washington American Society for Microbiology 01.05.2008
Subjects
Bacteria
Bacteriology
Biochemistry
Glycoproteins
Glycosylation
Mass spectrometry
Online AccessGet full text

Cover

More Information
Summary: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. [PUBLICATION ABSTRACT]
ISSN:0021-9193
1098-5530