Evidence for Covalent Attachment of Diphytanylglyceryl Phosphate to the Cell-surface Glycoprotein of Halobacterium halobium *

  title={Evidence for Covalent Attachment of Diphytanylglyceryl Phosphate to the Cell-surface Glycoprotein of Halobacterium halobium *},
  author={Akihiro Kikuchi and Hiroshi Sagami and Kyozo Ogura},
  journal={The Journal of Biological Chemistry},
  pages={18011 - 18016}
In a previous study, we demonstrated the occurrence of novel proteins modified with a diphytanylglyceryl group in thioether linkage in Halobacterium halobium (Sagami, H., Kikuchi, A., and Ogura, K. (1995) J. Biol. Chem. 270, 14851–14854). In this study, we further investigated protein isoprenoid modification in this halobacterium using several radioactive tracers such as [3H]geranylgeranyl diphosphate. One of the radioactive bands observed on SDS-polyacrylamide gel electrophoresis corresponded… 

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Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation.
It is reported that the H. volcanii S-layer glycoprotein is modified by a derivative of mevalonic acid and that maturation of the protein was prevented upon treatment with mevinolin (lovastatin), an inhibitor of meValonic acid biosynthesis, suggesting that lipid modification of S- layer glycoproteins is a general property of halophilic archaea.
Post-translational modification of the S-layer glycoprotein occurs following translocation across the plasma membrane of the haloarchaeon Haloferax volcanii.
  • J. Eichler
  • Biology
    European journal of biochemistry
  • 2001
Pulse-chase radiolabeling and cell-fractionation studies were employed to reveal that newly synthesized S-layer glycoprotein undergoes a maturation step following translocation of the protein across the plasma membrane.
Identification of the S-layer glycoproteins and their covalently linked glycans in the halophilic archaeon Haloarcula hispanica.
The determination of the N- and O-glycan structure will be helpful for studying the diverse protein glycosylation pathways in archaea utilizing H. hispanica as a new model.
S-Layer Glycoproteins and Flagellins: Reporters of Archaeal Posttranslational Modifications
Use of these well-characterized reporter proteins in the genetically tractable model organisms has allowed dissection of the pathways and characterization of many of the enzymes responsible for these modifications, and questions related to the heterogeneity associated with given modifications, such as differential or modulated glycosylation are considered.
Haloarchaea use the mid cell as the main surface processing hotspot for cell elongation, division and shape determination, and it is suggested that archaeal homologs to the bacterial phos-phatidylserine synthase (PssA) and phosphatidolserine decarboxylase ( PssD) are involved in ArtA-dependent protein maturation.
Lipid Anchoring of Archaeosortase Substrates and Midcell Growth in Haloarchaea
It is suggested that haloarchaea use the midcell as the main surface processing hot spot for cell elongation, division, and shape determination and that archaeal homologs to the bacterial phosphatidylserine synthase (PssA) and phosphatidoserine decarboxylase ( PssD) are involved in ArtA-dependent protein maturation.
Permuting the PGF Signature Motif Blocks both Archaeosortase-Dependent C-Terminal Cleavage and Prenyl Lipid Attachment for the Haloferax volcanii S-Layer Glycoprotein
The first in vivo studies of a novel protein-anchoring pathway involving lipid modification of a peptidase-processed C terminus are reported, suggesting that ArtA is either directly or indirectly involved in a novel proteolysis-coupled, covalent lipid-mediated anchoring mechanism by prokaryotes.
Novel Cell Surface Anchoring Mechanism of Prokaryotic Secreted Protein
The SLG is anchored to the membrane via a covalent lipid anchor, the first C-terminal lipid-anchoring mechanism described for any prokaryote, and it is shown that this process is also ArtA-dependent and that the substrate conserved PGF motif is critical for processing and lipid anchoring.


A Novel Type of Protein Modification by Isoprenoid-derived Materials. DIPHYTANYLGLYCERYLATED PROTEINS IN HALOBACTERIA(*)
The results indicate that Halobacteria contains specific proteins with a novel type of modification of a cysteine residue of theprotein with a diphytanylglyceryl group in thioether linkage.
Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria.
The isolation and chemical characterization of lipid-linked precursors of these saccharides have the following new features: Rather than the bacterial undecaprenol, a C60-dolichol is the carrier lipid.
Novel isoprenoid modified proteins in Halobacteria.
Incorporation of [3H]mevalonic acid-derived materials into proteins was studied with extremely halophilic archaebacteria, Halobacterium halobium and Halobacteria cutirubrum and no radioactive farnesol was found on the chromatography.
Covalent binding of dolichyl phosphate to proteins in rat liver.
The results indicate the presence of covalently bound dolichyl phosphate in rat liver and a major protein band at 23 kDa and some minor bands with higher molecular masses were found to be associated with this lipid.
Protein and Carbohydrate Composition of the Cell Envelope of Halobacterium salinarium
The isolated cell envelope of Halobacterium salinarium strain 1 contained 15 to 20 proteins that were resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and indicated that all of the nonlipid carbohydrate of the cell envelope is covalently bound to protein.
Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
The primary structure and the glycosylation pattern of the S-layer glycoproteins from Haloferax volcanii and from Halobacterium halobium were compared and found to exhibit distinct differences, despite the fact that three-dimensional reconstructions from electron micrographs revealed no structural differences.
Structural (shape-maintaining) role of the cell surface glycoprotein of Halobacterium salinarium.
  • M. Mescher, J. Strominger
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1976
The obligate halophile, Halobacterium salinarium, maintains a rod-shaped morphology under normal growth conditions and morphological changes that accompany alteration of the structure of the glycoprotein by growth in the presence of bacitracin or its removal with proteolytic enzymes strongly suggest that it forms a rigid matrix at the cell surface.