Potassium uptake permease

Low affinity potassium transport system protein
Identifiers
Symbol KUP or TrkD
Pfam PF02705
InterPro IPR003855.
High affinity potassium transporter
Identifiers
Symbol HAK1
Pfam PF02705
InterPro IPR003855

The potassium (K+) uptake permease (KUP) family (TC# 2.A.72) is a member of the APC superfamily of secondary carriers.[1] Proteins of the KUP/HAK/KT family include the KUP (TrkD) protein of E. coli and homologues in both Gram-positive and Gram-negative bacteria. High affinity (20 μM) K+ uptake systems (Hak1, TC# 2.A.72.2.1) of the yeast Debaryomyces occidentalis as well as the fungus, Neurospora crassa, and several homologues in plants have been characterized. Arabidopsis thaliana and other plants possess multiple KUP family paralogues. While many plant proteins cluster tightly together, the Hak1 proteins from yeast as well as the two Gram-positive and Gram-negative bacterial proteins are distantly related on the phylogenetic tree for the KUP family.[2] All currently classified members of the KUP family can be found in the Transporter Classification Database.

Structure and function

Escherichia coli

The E. coli protein is 622 amino acyl residues long and has 12 established transmembrane spanners (440 residues) with a requisite hydrophilic, C-terminal domain of 182 residues, localized to the cytoplasmic side of the membrane.[3] Deletion of most of the hydrophilic domain reduces but does not abolish KUP transport activity. The function of the C-terminal domain is not known. The E. coli KUP protein is believed to be a secondary transporter. Uptake is blocked by protonophores such as CCCP (but not arsenate), and evidence for a proton symport mechanism has been presented.[4] The N. crassa protein was earlier shown to be a K+:H+ symporter, establishing that the KUP family consists of secondary carriers.

Yeast

The yeast high affinity (KM = 1 µM) K+ transporter Hak1 is 762 amino acyl residues long with 12 putative TMSs. Like the E. coli KUP protein, it possesses a C-terminal hydrophilic domain, probably localized to the cytoplasmic side of the membrane. Hak1 may be able to accumulate K+ 106-fold against a concentration gradient. The plant high and low affinity K+ transporters can complement K+ uptake defects in E. coli.

TRK

TRK transporters, responsible for the bulk of K+ accumulation in plants, fungi, and bacteria, mediate ion currents driven by the large membrane voltages (-150 to -250 mV) common to non-animal cells. Bacterial TRK proteins resemble K+ channels in their primary sequence, crystallize as membrane dimers having intramolecular K+-channel-like folding, and complex with a cytoplasmic collar formed of four RCK domains.[5] Fungal TRK proteins possess a large built-in regulatory domain and a highly conserved pair of transmembrane helices (TMSs 7 and 8, ahead of the C-terminus), postulated to facilitate intramembranal oligomerization.These fungal HAK proteins are chloride channels mediating efflux, a process suppressed by osmoprotective agents. It involve hydrophobic gating and resembles conduction by Cys-loop ligand-gated anion channels. Possibly, the tendency of hydrophobic or amphipathic transmembrane helices to self-organize into oligomers creates novel ionic pathways through membranes: hydrophobic nanopores, pathways of low selectivity governed by the chaotropic behavior of individual ionic species under the influence of membrane voltage.[5]

Transport reaction

The generalized transport reaction for members of the KUP family is:[2]

K+ (out) + energy → K+ (in).

See also

References

  1. ↑ Vastermark A, Wollwage S, Houle ME, Rio R, Saier MH (October 2014). "Expansion of the APC superfamily of secondary carriers". Proteins. 82 (10): 2797–811. doi:10.1002/prot.24643. PMC 4177346. PMID 25043943.
  2. 1 2 Saier, MH Jr. "2.A.72 The K+ Uptake Permease (KUP) Family". Transporter Classification Database.
  3. ↑ Sato Y, Nanatani K, Hamamoto S, Shimizu M, Takahashi M, Tabuchi-Kobayashi M, Mizutani A, Schroeder JI, Souma S, Uozumi N (May 2014). "Defining membrane spanning domains and crucial membrane-localized acidic amino acid residues for K⁺ transport of a Kup/HAK/KT-type Escherichia coli potassium transporter". Journal of Biochemistry. 155 (5): 315–23. doi:10.1093/jb/mvu007. PMID 24519967.
  4. ↑ Zakharyan E, Trchounian A (October 2001). "K+ influx by Kup in Escherichia coli is accompanied by a decrease in H+ efflux". FEMS Microbiology Letters. 204 (1): 61–4. doi:10.1111/j.1574-6968.2001.tb10863.x. PMID 11682179.
  5. 1 2 Pardo JP, González-Andrade M, Allen K, Kuroda T, Slayman CL, Rivetta A (December 2015). "A structural model for facultative anion channels in an oligomeric membrane protein: the yeast TRK (K(+)) system". Pflügers Archiv. 467 (12): 2447–60. doi:10.1007/s00424-015-1712-6. PMID 26100673.

Further reading

  • Nieves-Cordones, Manuel; Razzaq Al Shiblawi, Fouad; Sentenac, Hervé (2016). "Chapter 9. Roles and Transport of Sodium and Potassium in Plants". In Astrid, Sigel; Helmut, Sigel; Roland K.O., Sigel. The Alkali Metal Ions: Their Role in Life. Metal Ions in Life Sciences. 16. Springer. pp. 291–324. doi:10.1007/978-4-319-21756-7_9.
  • Fu HH, Luan S (January 1998). "AtKuP1: a dual-affinity K+ transporter from Arabidopsis". The Plant Cell. 10 (1): 63–73. PMID 9477572.
  • Quintero FJ, Blatt MR (September 1997). "A new family of K+ transporters from Arabidopsis that are conserved across phyla". FEBS Letters. 415 (2): 206–11. PMID 9350997.
  • Greiner T, Ramos J, Alvarez MC, Gurnon JR, Kang M, Van Etten JL, Moroni A, Thiel G (December 2011). "Functional HAK/KUP/KT-like potassium transporter encoded by chlorella viruses". The Plant Journal. 68 (6): 977–86. doi:10.1111/j.1365-313X.2011.04748.x. PMID 21848655.
  • Pyo YJ, Gierth M, Schroeder JI, Cho MH (June 2010). "High-affinity K(+) transport in Arabidopsis: AtHAK5 and AKT1 are vital for seedling establishment and postgermination growth under low-potassium conditions". Plant Physiology. 153 (2): 863–75. doi:10.1104/pp.110.154369. PMC 2879780. PMID 20413648.
  • Senn ME, Rubio F, Bañuelos MA, Rodríguez-Navarro A (November 2001). "Comparative functional features of plant potassium HvHAK1 and HvHAK2 transporters". The Journal of Biological Chemistry. 276 (48): 44563–9. doi:10.1074/jbc.M108129200. PMID 11562376.

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