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

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

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 comple...

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Bibliographic Details
Main Authors: Nies, Dietrich H., Salzer, Ralf, Herzberg, Martin, Biuković, Goran, Grüber, Gerhard, Müller, Volker, Averhoff, Beate
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2013
Subjects:
DRNTU::Science::Biological sciences::Microbiology
Online Access:https://hdl.handle.net/10356/99636
http://hdl.handle.net/10220/17455
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Institution: Nanyang Technological University
Language: English
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Summary: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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