Document Detail


Add salt, add sugar: N-glycosylation in Haloferax volcanii.
MedLine Citation:
PMID:  23356324     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii have, however, begun to correct this situation. A combination of bioinformatics, molecular biology, biochemical and mass spectrometry approaches have served to delineate the Agl pathway responsible for N-glycosylation of the S-layer glycoprotein, a reporter of this post-translational modification in Hfx. volcanii. More recently, differential N-glycosylation of the S-layer glycoprotein as a function of environmental salinity was demonstrated, showing that this post-translational modification serves an adaptive role in Hfx. volcanii. Furthermore, manipulation of the Agl pathway, together with the capability of Hfx. volcanii to N-glycosylate non-native proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.
Authors:
Lina Kaminski; Shai Naparstek; Lina Kandiba; Chen Cohen-Rosenzweig; Adi Arbiv; Zvia Konrad; Jerry Eichler
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemical Society transactions     Volume:  41     ISSN:  1470-8752     ISO Abbreviation:  Biochem. Soc. Trans.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7506897     Medline TA:  Biochem Soc Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  432-5     Citation Subset:  IM    
Affiliation:
Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
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