Analyse eines unkonventionellen Vitamin-Transporters

BIOspektrum volume 18, pages493–496(2012)Cite this article

Abstract

Förster resonance energy transfer (FRET) identifies the co-localization of fluorescent macromolecules on a nanometer scale. FRET between nonidentical and identical fluorophores is called HeteroFRET or HomoFRET, respectively. We applied FRET techniques to analyze the oligomeric state of the core component (BioY) of a bacterial biotin transporter. BioY was fused to fluorescent proteins suitable for Hetero- and HomoFRET analyses. Spectrometric and imaging experiments with living cells strongly support a model with oligomers of BioY as the functional state of the core unit.

This is a preview of subscription content, access via your institution.

Access options

Buy single article

Instant access to the full article PDF.

US$ 39.95

Tax calculation will be finalised during checkout.

Literatur

  1. [1]

    Rodionov DA, Hebbeln P, Eudes A et al. (2009) A novel class of modular transporters for vitamins in prokaryotes. J Bacteriol 191:42–51

    PubMed  Article  CAS  Google Scholar 

  2. [2]

    Eitinger T, Rodionov DA, Grote M et al. (2011) Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions. FEMS Microbiol Rev 35:3–67

    PubMed  Article  CAS  Google Scholar 

  3. [3]

    Erkens GB, Majsnerowska M, Ter Beek J et al. (2012) Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes. Biochemistry 51:4390–4396

    Article  CAS  Google Scholar 

  4. [4]

    Neubauer O, Reiffler C, Behrendt L et al. (2011) Interactions among the A and T units of an ECF-type biotin transporter analyzed by site-specific crosslinking. PLoS One 6:e29087

    PubMed  Article  CAS  Google Scholar 

  5. [5]

    Henderson GB, Zevely EM, Huennekens FM (1979) Mechanism of folate transport in Lactobacillus casei: evidence for a component shared with the thiamine and biotin transport systems. J Bacteriol 137:1308–1314

    PubMed  CAS  Google Scholar 

  6. [6]

    Zhang P, Wang J, Shi Y (2010) Structure and mechanism of the S component of a bacterial ECF transporter. Nature 468:717–720

    PubMed  Article  CAS  Google Scholar 

  7. [7]

    Erkens GB, Berntsson RP, Fulyani F et al. (2011) The structural basis of modularity in ECF-type ABC transporters. Nat Struct Mol Biol 18:755–760

    PubMed  Article  CAS  Google Scholar 

  8. [8]

    Hebbeln P, Rodionov DA, Alfandega A et al. (2007) Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module. Proc Natl Acad Sci USA 104:2909–2914

    PubMed  Article  Google Scholar 

  9. [9]

    Kirsch F, Frielingsdorf S, Pohlmann A et al. (2012) Essential amino acid residues of BioY reveal that dimers are the functional S unit of the Rhodobacter capsulatus biotin transporter. J Bacteriol 194 (im Druck), doi: 10.1128/JB.00683-12

  10. [10]

    Finkenwirth F, Neubauer O, Gunzenhäuser J et al. (2010) Subunit composition of an energy-coupling-factor-type biotin transporter analysed in living bacteria. Biochem J 431:373–380

    PubMed  CAS  Google Scholar 

  11. [11]

    Grecco HE, Verveer PJ (2011) FRET in cell biology: still shining in the age of super-resolution? ChemPhysChem 12:484–490

    PubMed  Article  CAS  Google Scholar 

  12. [12]

    Bader AN, Hoetzl EG, Hofman J et al. (2011) Homo-FRET imaging as a tool to quantify protein and lipid clustering. ChemPhysChem 12:475–483

    PubMed  Article  CAS  Google Scholar 

Download references

Author information

Affiliations

  1. Institut für Biologie/Molekulare Biophysik, Hu Berlin, Berlin, Germany

    Joanna Ziomkowska & Andreas Herrmann

  2. Institut für Biologie/Mikrobiologie, Hu Berlin, Berlin, Germany

    Franziska Kirsch & Thomas Eitinger

  3. Institut für Biologie/Molekulare Biophysik, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115, Berlin, Germany

    Joanna Ziomkowska & Andreas Herrmann

  4. Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestraße 117, D-10115, Berlin, Germany

    Franziska Kirsch & Thomas Eitinger

Authors
  1. Joanna Ziomkowska
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Franziska Kirsch
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Andreas Herrmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Thomas Eitinger
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Joanna Ziomkowska or Franziska Kirsch or Andreas Herrmann or Thomas Eitinger.

Additional information

Franziska Kirsch, Thomas Eitinger, Joanna Ziomkowska und Andreas Herrmann (v. l. n. r.)

Die Arbeitsgruppe von Andreas Herrmann beschäftigt sich mit Lipid- und Protein-Wechselwirkungen und deren Bedeutung für die Struktur und Dynamik von Membranen. Schwerpunkte in der Arbeitsgruppe von Thomas Eitinger bilden bakterielle Aufnahmesysteme, unter anderem verschiedene Vertreter der ECF-Transporter für Vitamine und Übergangsmetallionen.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Ziomkowska, J., Kirsch, F., Herrmann, A. et al. Analyse eines unkonventionellen Vitamin-Transporters. Biospektrum 18, 493–496 (2012). https://doi.org/10.1007/s12268-012-0220-x

Download citation