Evidence map›Paper›PMID 25202014›Full record

ArticleThe Journal of biological chemistry2014

Zinc and ATP binding of the hexameric AAA-ATPase PilF from Thermus thermophilus: role in complex stability, piliation, adhesion, twitching motility, and natural transformation.

Ralf Salzer, Martin Herzberg, Dietrich H Nies, Friederike Joos, Barbara Rathmann, Yvonne Thielmann, Beate Averhoff

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Ralf SalzerMolecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany.
Martin HerzbergMolecular Microbiology, Institute for Biology/Microbiology, Martin Luther University, 06120 Halle-Wittenberg, Germany.
Dietrich H NiesMolecular Microbiology, Institute for Biology/Microbiology, Martin Luther University, 06120 Halle-Wittenberg, Germany.
Friederike JoosDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany, and.
Barbara RathmannDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Yvonne ThielmannDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Beate AverhoffMolecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany,. Electronic address: averhoff@bio.uni-frankfurt.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The traffic AAA-ATPase PilF is essential for pilus biogenesis and natural transformation of Thermus thermophilus HB27. Recently, we showed that PilF forms hexameric complexes containing six zinc atoms coordinated by conserved tetracysteine motifs. Here we report that zinc binding is essential for complex stability. However, zinc binding is neither required for pilus biogenesis nor natural transformation. A number of the mutants did not exhibit any pili during growth at 64 °C but still were transformable. This leads to the conclusion that type 4 pili and the DNA translocator are distinct systems. At lower growth temperatures (55 °C) the zinc-depleted multiple cysteine mutants were hyperpiliated but defective in pilus-mediated twitching motility. This provides evidence that zinc binding is essential for the role of PilF in pilus dynamics. Moreover, we found that zinc binding is essential for complex stability but dispensable for ATPase activity. In contrast to many polymerization ATPases from mesophilic bacteria, ATP binding is not required for PilF complex formation; however, it significantly increases complex stability. These data suggest that zinc and ATP binding increase complex stability that is important for functionality of PilF under extreme environmental conditions.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAdenylyl ImidodiphosphateAmino Acid MotifsAmino Acid SubstitutionBacterial AdhesionBacterial ProteinsCysteineEnzyme StabilityFimbriae, BacterialProtein BindingProtein MultimerizationThermus thermophilusTransformation, BacterialZincAdenosine TriphosphatasesAdenosine TriphosphateAdenylyl ImidodiphosphateBacterial ProteinsCysteineZincATPases Associated with Diverse Cellular Activities (AAA)Cell MotilityDNA TransformationType IV PiliZinc

Identifiers

PMID25202014
PMCPMC4215219

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.