Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Proteomics Analysis of Thermoplasma Quinone Droplets.

Nagy, I., Sun, N., Varga, S., Boicu, M., Zinzula, L., & Kukolya, J. (2019). Proteomics Analysis of Thermoplasma Quinone Droplets. Proteomics, 19(3): 1800317. doi:10.1002/pmic.201800317.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Nagy, Istvan1, Autor           
Sun, Na1, Autor           
Varga, Sandor2, Autor
Boicu, Marius1, Autor           
Zinzula, Luca1, Autor           
Kukolya, Jozsef2, Autor
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: 1D PAGE; LC-MS/MS; Thermoplasma Quinone droplets; Thermoplasma acidophilum
 Zusammenfassung: A novel type of lipid droplet/lipoprotein (LD/LP) particle from Thermoplasma acidophilum has been identified recently, and based on biochemical evidences, it was named Thermoplasma Quinone Droplet (TaQD). The major components of TaQDs are menaquinones, and to some extent polar lipids, and the 153 amino acid long Ta0547 vitellogenin-N domain protein. In this paper, the aim is to identify TaQD proteome components with 1D-SDS-PAGE/LC-MS/MS and cross reference them with Edman degradation. TaQD samples isolated with three different purification methods-column chromatography, immunoprecipitation, and LD ultracentrifugation-are analyzed. Proteins Ta0093, Ta0182, Ta0337, Ta0437, Ta0438, Ta0547, and Ta1223a are identified as constituents of the TaQD proteome. The majority of these proteins is uncharacterized and has low molecular weight, and none of them is predicted to take part in lipid metabolism. Bioinformatics analyses does not predict any interaction between these proteins, however, there are indications of interactions with proteins taking part in lipid metabolism. Whether if TaQDs provide platform for lipid metabolism and the interactions between TaQD proteins and lipid metabolism proteins occur in the reality remain for further studies. © 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2018-122019-02
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 30520262
DOI: 10.1002/pmic.201800317
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Proteomics
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Weinheim : WILEY-VCH
Seiten: - Band / Heft: 19 (3) Artikelnummer: 1800317 Start- / Endseite: - Identifikator: ISSN: 1615-9853
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000294310