Metal-binding properties of the N-terminal intrinsically disordered region of the membrane protein PcoB involved in bacterial copper homeostasis. - 2026
[en] Intrinsically disordered regions (IDRs) participate in many protein functions, yet their contribution to metal resistance remains mostly unexplored. In Caulobacter vibrioides, the copper (Cu) efflux protein PcoB harbors a disordered N-terminal domain (NTD). Here, we have investigated the metal-binding properties of the NTD to elucidate its role in C. vibrioides Cu(II) regulation. To this end, AlphaFold3 modeling and sequence-based analysis along with biophysical characterization were performed. The structural properties of recombinant NTD were assessed by circular dichroism (CD), size-exclusion chromatography coupled with multi-angle light scattering (SEC-MALS), and nuclear magnetic resonance (NMR) spectroscopy. PcoB NTD was shown to be monomeric in solution, highly disordered, and retaining a highly populated transient 13-residue α-helix near its C-terminus. Interactions with seven divalent metal cations were evaluated at pH 7.5, 5.5, and 4.5 using intrinsic tyrosine fluorescence (ITyrF), isothermal titration calorimetry (ITC), and NMR. At pH 7.5, the NTD weakly bound Cu(II), Co(II), Ni(II), and Zn(II) ions, whereas under acidic conditions, only Cu(II) binding persisted with a reduced stoichiometry. These results suggest a pH-dependent modulation of the metal-coordination mechanism, Cu(II) displaying a distinct behavior likely driven by the protonation sensitivity of histidine residues and contribution from acidic residues distributed along the sequence. We propose that the disordered NTD acts as a catch-and-deliver arm that captures Cu(II) ions in the periplasm and guides them towards the β-barrel for export. These findings provide a mechanistic framework for PcoB NTD metal handling and, more broadly, how membrane IDRs mediate environment-sensitive periplasmic interactions.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bâlon, Hugo; Laboratory of Physical Chemistry of Biomolecules, UCPTS, University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium. Electronic address: hugo.balon@unamur.be
Rouxhet, Simon; Laboratory of Physical Chemistry of Biomolecules, UCPTS, University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium
Mignon, Julien; Laboratory of Physical Chemistry of Biomolecules, UCPTS, University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium
Prestel, Andreas; Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark
Kragelund, Birthe B; Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark
Matroule, Jean-Yves ; Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Virologie - Immunologie ; Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Research Unit in Microorganisms Biology (URBM), Department of Biology, Namur, Belgium
Michaux, Catherine; Laboratory of Physical Chemistry of Biomolecules, UCPTS, University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium. Electronic address: catherine.michaux@unamur.be
Language :
English
Title :
Metal-binding properties of the N-terminal intrinsically disordered region of the membrane protein PcoB involved in bacterial copper homeostasis.
Publication date :
April 2026
Journal title :
International Journal of Biological Macromolecules
FRIA - Fund for Research Training in Industry and Agriculture NNF - Novo Nordisk Foundation Villum Fonden F.R.S.-FNRS - Fonds de la Recherche Scientifique
Funding text :
H. B. and S. R. thank the Belgian National Fund for Scientific Research (F.R.S.-FNRS) for their FRIA (Fund for Research training in Industry and Agriculture) Doctoral grant and C. M. for her Senior Research Associate position. Authors are appreciative of the University of Namur Mass Spectrometry platform (MaSUN) as well as to the Technological Platform Optics, Lasers and Spectroscopy (LOS). We also acknowledge the Robotein\u00AE platform of the BE Instruct-ERIC Centre for providing access to their equipment. Finally, authors are also grateful to the Research Unit in Biology of Micro-organisms for the overexpression infrastructures and H. B. especially thanks Marine Ote for her precious help concerning all the cloning aspect of the NTD mutant. B.B.K. thank the Novo Nordisk Foundation (grant no. NNF18OC0033926 and NNF18OC0032996 ) and Villum Fonden for support.
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