Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1995 Sep;109(1):327–330. doi: 10.1104/pp.109.1.327

Evidence that plant K+ channel proteins have two different types of subunits.

H Tang 1, A C Vasconcelos 1, G A Berkowitz 1
PMCID: PMC157592  PMID: 7480329

Abstract

Plant K+ channel proteins have been previously characterized as tetramers of membrane-spanning alpha subunit polypeptides. Recent studies have identified a 39-kD, hydrophilic polypeptide that is a structural component of purified animal K+ channel proteins. We have cloned and sequenced an Arabidopsis thaliana cDNA encoding a 38.4-kD polypeptide that has a sequence homologous to the animal K+ channel beta subunit. Southern and northern analyses indicate the presence of a gene encoding this cDNA in the Arabidopsis genome and that its transcription product is present in Arabidopsis cells. To our knowledge, this is the first report to document the presence of K+ channel beta subunits in plants.

Full Text

The Full Text of this article is available as a PDF (1.6 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson J. A., Huprikar S. S., Kochian L. V., Lucas W. J., Gaber R. F. Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3736–3740. doi: 10.1073/pnas.89.9.3736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dolly J. O., Rettig J., Scott V. E., Parcej D. N., Wittkat R., Sewing S., Pongs O. Oligomeric and subunit structures of neuronal voltage-sensitive K+ channels. Biochem Soc Trans. 1994 May;22(2):473–478. doi: 10.1042/bst0220473. [DOI] [PubMed] [Google Scholar]
  3. Jan L. Y., Jan Y. N. Potassium channels and their evolving gates. Nature. 1994 Sep 8;371(6493):119–122. doi: 10.1038/371119a0. [DOI] [PubMed] [Google Scholar]
  4. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  5. Muniz Z. M., Diniz C. R., Dolly J. O. Characterisation of binding sites for delta-dendrotoxin in guinea-pig synaptosomes: relationship to acceptors for the K+-channel probe alpha-dendrotoxin. J Neurochem. 1990 Jan;54(1):343–346. doi: 10.1111/j.1471-4159.1990.tb13320.x. [DOI] [PubMed] [Google Scholar]
  6. Muniz Z. M., Parcej D. N., Dolly J. O. Characterization of monoclonal antibodies against voltage-dependent K+ channels raised using alpha-dendrotoxin acceptors purified from bovine brain. Biochemistry. 1992 Dec 15;31(49):12297–12303. doi: 10.1021/bi00164a003. [DOI] [PubMed] [Google Scholar]
  7. Parcej D. N., Dolly J. O. Dendrotoxin acceptor from bovine synaptic plasma membranes. Binding properties, purification and subunit composition of a putative constituent of certain voltage-activated K+ channels. Biochem J. 1989 Feb 1;257(3):899–903. doi: 10.1042/bj2570899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Parcej D. N., Scott V. E., Dolly J. O. Oligomeric properties of alpha-dendrotoxin-sensitive potassium ion channels purified from bovine brain. Biochemistry. 1992 Nov 17;31(45):11084–11088. doi: 10.1021/bi00160a018. [DOI] [PubMed] [Google Scholar]
  9. Rettig J., Heinemann S. H., Wunder F., Lorra C., Parcej D. N., Dolly J. O., Pongs O. Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit. Nature. 1994 May 26;369(6478):289–294. doi: 10.1038/369289a0. [DOI] [PubMed] [Google Scholar]
  10. Schachtman D. P., Schroeder J. I., Lucas W. J., Anderson J. A., Gaber R. F. Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA. Science. 1992 Dec 4;258(5088):1654–1658. doi: 10.1126/science.8966547. [DOI] [PubMed] [Google Scholar]
  11. Schauf C. L., Wilson K. J. Properties of Single K and Cl Channels in Asclepias tuberosa Protoplasts. Plant Physiol. 1987 Oct;85(2):413–418. doi: 10.1104/pp.85.2.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schroeder J. I., Ward J. M., Gassmann W. Perspectives on the physiology and structure of inward-rectifying K+ channels in higher plants: biophysical implications for K+ uptake. Annu Rev Biophys Biomol Struct. 1994;23:441–471. doi: 10.1146/annurev.bb.23.060194.002301. [DOI] [PubMed] [Google Scholar]
  13. Scott V. E., Parcej D. N., Keen J. N., Findlay J. B., Dolly J. O. Alpha-dendrotoxin acceptor from bovine brain is a K+ channel protein. Evidence from the N-terminal sequence of its larger subunit. J Biol Chem. 1990 Nov 25;265(33):20094–20097. [PubMed] [Google Scholar]
  14. Scott V. E., Rettig J., Parcej D. N., Keen J. N., Findlay J. B., Pongs O., Dolly J. O. Primary structure of a beta subunit of alpha-dendrotoxin-sensitive K+ channels from bovine brain. Proc Natl Acad Sci U S A. 1994 Mar 1;91(5):1637–1641. doi: 10.1073/pnas.91.5.1637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  16. Sussman M. R. Shaking Arabidopsis thaliana. Science. 1992 May 1;256(5057):619–619. doi: 10.1126/science.256.5057.619. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES