AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii

Hilla Magidovich, Sophie Yurist-Doutsch, Zvia Konrad, Valeria V. Ventura, Anne Dell, Paul G. Hitchen, Jerry Eichler

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

While pathways for N-glycosylation in Eukarya and Bacteria have been solved, considerably less is known of this post-translational modification in Archaea. In the halophilic archaeon Haloferax volcanii, proteins encoded by the agl genes are involved in the assembly and attachment of a pentasaccharide to select asparagine residues of the S-layer glycoprotein. AglP, originally identified based on the proximity of its encoding gene to other agl genes whose products were shown to participate in N-glycosylation, was proposed, based on sequence homology, to serve as a methyltransferase. In the present report, gene deletion and mass spectrometry were employed to reveal that AglP is responsible for adding a 14 Da moiety to a hexuronic acid found at position four of the pentasaccharide decorating the Hfx. volcanii S-layer glycoprotein. Subsequent purification of a tagged version of AglP and development of an in vitro assay to test the function of the protein confirmed that AglP is a S-adenosyl-L- methionine-dependent methyltransferase.

Original languageEnglish
Pages (from-to)190-199
Number of pages10
JournalMolecular Microbiology
Volume76
Issue number1
DOIs
StatePublished - 1 Jan 2010

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