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  Lipoprotein-like particles in a prokaryote: quinone droplets of Thermoplasma acidophilum

Nagy, I., Knispel, R. W., Kofler, C., Orsini, M., Boicu, M., Varga, S., et al. (2016). Lipoprotein-like particles in a prokaryote: quinone droplets of Thermoplasma acidophilum. FEMS Microbiology Letters, 363(18): fnw169. doi:10.1093/femsle/fnw169.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-8F9F-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-8FA0-6
Genre: Journal Article

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 Creators:
Nagy, Istvan1, Author              
Knispel, Roland Wilhelm1, Author              
Kofler, Christine1, Author              
Orsini, Massimiliano2, Author
Boicu, Marius1, Author              
Varga, Sandor2, Author
Weyher-Stingl, Elisabeth3, Author              
Sun, Na1, Author              
Fernandez-Busnadiego, Ruben1, Author              
Kukolya, Jozsef2, Author
Nickell, Stephan1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              
3Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: LIPOVITELLIN; BIOCHEMISTRY; PROTEINS; LIPIDSMicrobiology; thermo-acidophilic archaeon; quinone droplet; vitamin K2-7; Ta0547; vitellogenin-N domain protein;
 Abstract: Cytosolic, globular droplets with an average diameter of 50 nm were observed in vitrified Thermoplasma acidophilum cells by means of cryo-electron tomography. These droplets were isolated by column chromatography and immunoprecipitation protein purification methods. Subsequent chemical and biochemical analyses identified lipid and protein components, respectively. Two major lipid components, comigrating menaquinones at the solvent front and the slower migrating Thermoplasma polar lipid U4, were detected by TLC experiments. The major protein component was identified as the 153 amino acid long Ta0547 vitellogenin-N domain protein. This domain has been found so far exclusively in large lipid transport proteins of vertebrates and non-vertebrates. Blast protein database homology searches with Ta0547 did not return any eukaryal hits; homologous sequences were found only in thermo-acidophilic archaeons. However, a profile-sequence domain search performed with the vitellogenin-N domain (PF01347) hmm-profile against the T. acidophilum proteome returned Ta0547 as hit. Electron microscopy appearance of isolated droplets resembled to lipoprotein particles. However, no (tetraether) lipid layer could be detected on the droplets surface, rather hydrophobic compounds of the electron dense lumen were surrounded by a denser discontinuous protein boundary. Based on described features, these particles qualify for a novel lipoprotein particle category, what we nominated Thermoplasma Quinone Droplet.

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Language(s): eng - English
 Dates: 2016-07-112016-09
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000388379400001
DOI: 10.1093/femsle/fnw169
 Degree: -

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Title: FEMS Microbiology Letters
  Other : FEMS Microbiol. Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Oxford
Pages: - Volume / Issue: 363 (18) Sequence Number: fnw169 Start / End Page: - Identifier: ISSN: 0378-1097
CoNE: /journals/resource/954925484705