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Fluoride-dependent interruption of the transport cycle of a CLC Cl−/H+ antiporter

Lim, Hyun-Ho, Stockbridge, Randy B, Miller, Christopher·2013·Nature Chemical Biology
DOI 10.1038/nchembio.1336PMC PMC3805709
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  • A bacterial Cl−/H+ CLC antiporter is potently inhibited when the protonated gating glutamate hydrogen bonds with a F− in the anion binding site, locking down the glutamate and interrupting the transport cycle.

    “As a mechanistic counterpoint to the CLCFs, a bacterial Cl−/H+ CLC antiporter is potently inhibited when the protonated gating glutamate hydrogen bonds with a F− in the anion binding site, “locking down” the glutamate and interrupting the transport cycle(58, 59).”

    From Membrane exporters of fluoride ion (2021) · cites this paper as [58]

  • Additional CLC homologs for chloride transport are not capable of transporting fluoride.

    “Many bacteria also possess additional CLC homologs for chloride transport; these are not capable of transporting fluoride80.”

    From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [80]

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Research works printed but not linked: 38

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  2. Steinmeyer, K. et al. Inactivation of muscle chloride channel by transposon insertion in mytotonic mice. Nature 354, 304–308 (1991). · DOI
  3. Günther, W., Luchow, A., Cluzeaud, F., Vandewalle, A. & Jentsch, T.J. ClC-5, the chloride channel mutated in Dent′s disease, colocalizes with the proton pump in endocytotically active kidney cells. Proc. Natl. Acad. Sci. USA 95, 8075–8080 (1998). · DOI
  4. Steinberg, B.E. et al. A cation counterflux supports lysosomal acidification. J. Cell Biol. 189, 1171–1186 (2010). · DOI
  5. De Angeli, A. et al. AtCLCa, a proton/nitrate antiporter, mediates nitrate accumulation in plant vacuoles. Nature 442, 939–942 (2006). · DOI
  6. Iyer, R., Iverson, T.M., Accardi, A. & Miller, C. A biological role for prokaryotic ClC chloride channels. Nature 419, 715–718 (2002). · DOI
  7. Jentsch, T.J., Steinmeyer, K. & Schwarz, G. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348, 510–514 (1990). · DOI
  8. Accardi, A. & Miller, C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl− channels. Nature 427, 803–807 (2004). · DOI
  9. Miller, C. ClC chloride channels viewed through a transporter lens. Nature 440, 484–489 (2006). · DOI
  10. Fahlke, C., Durr, C. & George, A.L. Mechanism of ion permeation in skeletal muscle chloride channels. J. Gen. Physiol. 110, 551–564 (1997). · DOI
  11. Rychkov, G.Y., Pusch, M., Roberts, M.L., Jentsch, T.J. & Bretag, A.H. Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions. J. Gen. Physiol. 111, 653–665 (1998). · DOI
  12. Maduke, M., Pheasant, D.J. & Miller, C. High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J. Gen. Physiol. 114, 713–722 (1999). · DOI
  13. Nguitragool, W. & Miller, C. Uncoupling of a CLC Cl−/H+ exchange transporter by polyatomic anions. J. Mol. Biol. 362, 682–690 (2006). · DOI
  14. De Stefano, S., Pusch, M. & Zifarelli, G. Extracellular determinants of anion discrimination of the Cl−/H+ antiporter protein CLC-5. J. Biol. Chem. 286, 44134–44144 (2011). · DOI
  15. Fahlke, C. Ion permeation and selectivity in ClC-type chloride channels. Am. J. Physiol. Renal Physiol. 280, F748–F757 (2001). · DOI
  16. Baker, J.L. et al. Widespread genetic switches and toxicity resistance proteins for fluoride. Science 335, 233–235 (2012). · DOI · Paper page
  17. Stockbridge, R.B. et al. Fluoride resistance and transport by riboswitch-controlled CLC antiporters. Proc. Natl. Acad. Sci. USA 109, 15289–15294 (2012). · DOI · Paper page
  18. Walden, M. et al. Uncoupling and turnover in a Cl−/H+ exchange transporter. J. Gen. Physiol. 129, 317–329 (2007). · DOI · Paper page
  19. Picollo, A., Malvezzi, M., Houtman, J.C. & Accardi, A. Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters. Nat. Struct. Mol. Biol. 16, 1294–1301 (2009). · DOI
  20. Lobet, S. & Dutzler, R. Ion binding properties of the CLC chloride selectivity filter. EMBO J. 25, 24–33 (2006). · DOI
  21. Picollo, A., Xu, Y., Johner, N., Berneche, S. & Accardi, A. Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H+:Cl− exchanger. Nat. Struct. Mol. Biol. 19, 525–531 (2012). · DOI
  22. Accardi, A. et al. Separate ion pathways in a Cl−/H+ exchanger. J. Gen. Physiol. 126, 563–570 (2005). · DOI
  23. Faraldo-Gómez, J.D. & Roux, B. Electrostatics of ion stabilization in a ClC chloride channel homologue from Escherichia coli. J. Mol. Biol. 339, 981–1000 (2004). · DOI
  24. Jayaram, H., Robertson, J.L., Wu, F., Williams, C. & Miller, C. Structure of a slow CLC Cl/H+ antiporter from a cyanobacterium. Biochemistry 50, 788–794 (2011). · DOI
  25. Accardi, A., Lobet, S., Williams, C., Miller, C. & Dutzler, R. Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691–699 (2006). · DOI · Paper page
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  27. Feng, L., Campbell, E.B., Hsiung, Y. & MacKinnon, R. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330, 635–641 (2010). · DOI · Paper page
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Metadata

Authors
Lim, H.-H., Stockbridge, R. B., & Miller, C.
Venue
Nature Chemical Biology
Publisher
Springer Science and Business Media LLC
Published
2013-09-15
Volume
9
Issue
11
Pages
721-725
ISSN
  • 1552-4450
  • 1552-4469
DOI
10.1038/nchembio.1336
PMC
PMC3805709
Cited by
43
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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