Accession Number:

ADA515568

Title:

Protein Glycosylation in Archaea: A Post-Translational Modification to Enhance Extremophilic Protein Stability

Descriptive Note:

Final rept. 1 Jan 2007-30 Nov 2009

Corporate Author:

BEN-GURION UNIV OF THE NEGEV BEERSHEBA (ISRAEL)

Personal Author(s):

• Eichler, Jerry

Report Date:

2010-01-15

Pagination or Media Count:

27.0

Abstract:

Post-translational modifications account for much of the biological diversity generated at the proteome level. Of these, glycosylation is the most prevalent. Long-thought to be unique to Eukarya, it is now clear that both Bacteria and Archaea are also capable of N-glycosylation, namely the covalent linkage of oligosaccharides to select target asparagine residues. However, little had been known of this process in Archaea. As such, this project aimed at defining the N-glycosylation pathway of the halophilic archaeon Haloferax volcanii. Employing a combination of bioinformatics, genetic, biochemical and structural approaches, the funded research succeeded in identifying a group of clustered H. volcanii genes the agl genes encoding proteins involved in the assembly and attachment of a pentasaccharide to select asparagine residues of the S-layer glycoprotein, a reporter of N-glycosylation in this species. In addition to providing insight into N-glycosylation across evolution and the biology of extremophiles, these findings could be exploited to create archaeal strains expressing selected N-glycosylation enzyme modules. This would allow for a harnessing of the greater diversity associated with this post-translational modification in Archaea in the design of tailor-made glycoproteins.

Descriptors:

• *GLYCOPROTEINS
• *MICROORGANISMS
• ENZYMES
• CARBOHYDRATES
• GENES
• BIOCHEMISTRY
• MODIFICATION

Subject Categories:

• Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE