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The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content

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The Original Article was published on 06 January 2011

Abstract

The DNA-translocator ATPase PilF of Thermus thermophilus HB27 is a hexamer built by six identical subunits. Despite the presence of a conserved zinc-binding site in every subunit, only one zinc atom per hexamer was found. Re-examination of the zinc content of PilF purified from cells grown in complex media with different lots of yeast extract revealed six zinc atoms per hexamer. These data demonstrate that the low zinc content reported before was most likely a result of zinc depletion of the yeast extract used.

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Acknowledgments

This study was supported by a grant from the Deutsche Forschungsgemeinschaft (AV 9/6-1).

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Authors and Affiliations

  1. Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt am Main, Germany

    Ralf Salzer, Volker Müller & Beate Averhoff

  2. Molecular Microbiology, Institute for Biology/Microbiology, Martin Luther University, Halle-Wittenberg, Germany

    Martin Herzberg & Dietrich H. Nies

  3. School of Biological Sciences, Nanyang Technological University, Singapore, 637551, Republic of Singapore

    Goran Biuković & Gerhard Grüber

Authors
  1. Ralf Salzer
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  2. Martin Herzberg
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  3. Dietrich H. Nies
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  4. Goran Biuković
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  5. Gerhard Grüber
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  6. Volker Müller
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  7. Beate Averhoff
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Corresponding author

Correspondence to Beate Averhoff.

Additional information

Communicated by A. Driessen.

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Salzer, R., Herzberg, M., Nies, D.H. et al. The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content. Extremophiles 17, 697–698 (2013). https://doi.org/10.1007/s00792-013-0544-6

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  • DOI: https://doi.org/10.1007/s00792-013-0544-6

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