Document Detail


Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation.
MedLine Citation:
PMID:  22029420     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To cope with life in hypersaline environments, halophilic archaeal proteins are enriched in acidic amino acids. This strategy does not, however, offer a response to transient changes in salinity, as would post-translational modifications. To test this hypothesis, N-glycosylation of the Haloferax volcanii S-layer glycoprotein was compared in cells grown in high (3.4 M NaCl) and low (1.75 M NaCl) salt, as was the glycan bound to dolichol phosphate, the lipid upon which the N-linked glycan is assembled. In high salt, S-layer glycoprotein Asn-13 and Asn-83 are modified by a pentasaccharide, while dolichol phosphate is modified by a tetrasaccharide comprising the first four pentasaccharide residues. When the same targets were considered from cells grown in low salt, substantially less pentasaccharide was detected. At the same time, cells grown at low salinity contain dolichol phosphate modified by a distinct tetrasaccharide absent in cells grown at high salinity. The same tetrasaccharide modified S-layer glycoprotein Asn-498 in cells grown in low salt, whereas no glycan decorated this residue in cells grown in the high-salt medium. Thus, in response to changes in environmental salinity, Hfx. volcanii not only modulates the N-linked glycans decorating the S-layer glycoprotein but also the sites of such post-translational modification.
Authors:
Ziqiang Guan; Shai Naparstek; Doron Calo; Jerry Eichler
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-10-26
Journal Detail:
Title:  Environmental microbiology     Volume:  14     ISSN:  1462-2920     ISO Abbreviation:  Environ. Microbiol.     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-03-05     Completed Date:  2012-09-07     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  100883692     Medline TA:  Environ Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  743-53     Citation Subset:  IM    
Copyright Information:
© 2011 Society for Applied Microbiology and Blackwell Publishing Ltd.
Affiliation:
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
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MeSH Terms
Descriptor/Qualifier:
Archaeal Proteins / genetics,  metabolism
Dolichol Phosphates / metabolism
Glycoproteins / genetics,  metabolism*
Glycosylation
Haloferax volcanii / genetics,  metabolism,  physiology*
Membrane Glycoproteins
Oligosaccharides / metabolism
Polysaccharides / metabolism
Protein Processing, Post-Translational
Salinity
Salt-Tolerance / physiology*
Sodium Chloride / metabolism
Grant Support
ID/Acronym/Agency:
GM-069338/GM/NIGMS NIH HHS; U54 GM069338/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Archaeal Proteins; 0/Dolichol Phosphates; 0/Glycoproteins; 0/Membrane Glycoproteins; 0/Oligosaccharides; 0/Polysaccharides; 0/S-layer proteins; 7647-14-5/Sodium Chloride
Comments/Corrections

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