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

@article{Kikuchi1999EvidenceFC,
  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},
  year={1999},
  volume={274},
  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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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.
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Lipid Anchoring of Archaeosortase Substrates and Midcell Growth in Haloarchaea
TLDR
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
TLDR
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Novel Cell Surface Anchoring Mechanism of Prokaryotic Secreted Protein
TLDR
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References

SHOWING 1-10 OF 27 REFERENCES
A Novel Type of Protein Modification by Isoprenoid-derived Materials. DIPHYTANYLGLYCERYLATED PROTEINS IN HALOBACTERIA(*)
TLDR
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.
TLDR
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.
TLDR
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.
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
...
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