Document Detail


A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.
MedLine Citation:
PMID:  22469971     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In N-glycosylation in both Eukarya and Archaea, N-linked oligosaccharides are assembled on dolichol phosphate prior to transfer of the glycan to the protein target. However, whereas only the α-position isoprene subunit is saturated in eukaryal dolichol phosphate, both the α- and ω-position isoprene subunits are reduced in the archaeal lipid. The agents responsible for dolichol phosphate saturation remain largely unknown. The present study sought to identify dolichol phosphate reductases in the halophilic archaeon, Haloferax volcanii. Homology-based searches recognize HVO_1799 as a geranylgeranyl reductase. Mass spectrometry revealed that cells deleted of HVO_1799 fail to fully reduce the isoprene chains of H. volcanii membrane phospholipids and glycolipids. Likewise, the absence of HVO_1799 led to a loss of saturation of the ω-position isoprene subunit of C(55) and C(60) dolichol phosphate, with the effect of HVO_1799 deletion being more pronounced with C(60) dolichol phosphate than with C(55) dolichol phosphate. Glycosylation of dolichol phosphate in the deletion strain occurred preferentially on that version of the lipid saturated at both the α- and ω-position isoprene subunits.
Authors:
Shai Naparstek; Ziqiang Guan; Jerry Eichler
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-03-24
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1821     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-04-30     Completed Date:  2013-01-31     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  923-33     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier B.V. All rights reserved.
Affiliation:
Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Archaeal Proteins / genetics,  metabolism*
Butadienes / chemistry,  metabolism
Cell Membrane / chemistry,  metabolism
Chromatography, Liquid
Dolichol Phosphates / chemistry,  metabolism*
Gene Deletion
Glycolipids / chemistry,  metabolism
Haloferax volcanii / enzymology,  genetics,  metabolism*
Hemiterpenes / chemistry,  metabolism
Membrane Lipids / chemistry,  metabolism
Molecular Sequence Data
Oxidoreductases / genetics,  metabolism*
Pentanes / chemistry,  metabolism
Phospholipids / chemistry,  metabolism
Sequence Homology, Amino Acid
Spectrometry, Mass, Electrospray Ionization
Tandem Mass Spectrometry
Grant Support
ID/Acronym/Agency:
GM-069338/GM/NIGMS NIH HHS; R01 GM051310-14/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Archaeal Proteins; 0/Butadienes; 0/Dolichol Phosphates; 0/Glycolipids; 0/Hemiterpenes; 0/Membrane Lipids; 0/Pentanes; 0/Phospholipids; 0A62964IBU/isoprene; EC 1.-/Oxidoreductases; EC 1.3.1.-/geranylgeranyl reductase
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