Skip to main content

A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.

Publication ,  Journal Article
Naparstek, S; Guan, Z; Eichler, J
Published in: Biochim Biophys Acta
June 2012

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.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 2012

Volume

1821

Issue

6

Start / End Page

923 / 933

Location

Netherlands

Related Subject Headings

  • Tandem Mass Spectrometry
  • Spectrometry, Mass, Electrospray Ionization
  • Sequence Homology, Amino Acid
  • Phospholipids
  • Pentanes
  • Oxidoreductases
  • Molecular Sequence Data
  • Membrane Lipids
  • Hemiterpenes
  • Haloferax volcanii
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Naparstek, S., Guan, Z., & Eichler, J. (2012). A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii. Biochim Biophys Acta, 1821(6), 923–933. https://doi.org/10.1016/j.bbalip.2012.03.002
Naparstek, Shai, Ziqiang Guan, and Jerry Eichler. “A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.Biochim Biophys Acta 1821, no. 6 (June 2012): 923–33. https://doi.org/10.1016/j.bbalip.2012.03.002.
Naparstek, Shai, et al. “A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.Biochim Biophys Acta, vol. 1821, no. 6, June 2012, pp. 923–33. Pubmed, doi:10.1016/j.bbalip.2012.03.002.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

June 2012

Volume

1821

Issue

6

Start / End Page

923 / 933

Location

Netherlands

Related Subject Headings

  • Tandem Mass Spectrometry
  • Spectrometry, Mass, Electrospray Ionization
  • Sequence Homology, Amino Acid
  • Phospholipids
  • Pentanes
  • Oxidoreductases
  • Molecular Sequence Data
  • Membrane Lipids
  • Hemiterpenes
  • Haloferax volcanii