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

Ralf Salzer; Martin Herzberg; Dietrich H Nies; Goran Biuković; Gerhard Grüber; Volker Müller; Beate Averhoff

doi:10.1007/s00792-013-0544-6

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

Extremophiles. 2013 Jul;17(4):697-8. doi: 10.1007/s00792-013-0544-6. Epub 2013 May 28.

Authors

Ralf Salzer¹, Martin Herzberg, Dietrich H Nies, Goran Biuković, Gerhard Grüber, Volker Müller, Beate Averhoff

Affiliation

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

PMID: 23712905
DOI: 10.1007/s00792-013-0544-6

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism
Binding Sites
DNA / metabolism
Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins / chemistry*
Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins / metabolism
Protein Subunits / chemistry
Protein Subunits / metabolism
Thermus thermophilus / enzymology*
Zinc / analysis*

Substances

Bacterial Proteins
Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins
Protein Subunits
DNA
Zinc