Evidence That Plant K+ Channel Proteins Have Two Different Types of Subunits
Open Access
- 1 September 1995
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 109 (1) , 327-330
- https://doi.org/10.1104/pp.109.1.327
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.Keywords
This publication has 15 references indexed in Scilit:
- Detection of specific sequences among DNA fragments separated by gel electrophoresisPublished by Elsevier ,2006
- Potassium channels and their evolving gatesNature, 1994
- Perspectives on the Physiology and Structure of Inward-Rectifying K+ Channels in Higher Plants: Biophysical Implications for K+ UptakeAnnual Review of Biophysics, 1994
- Primary structure of a beta subunit ofalpha-dendrotoxin-sensitive K+ channels from bovine brain.Proceedings of the National Academy of Sciences, 1994
- Characterization of monoclonal antibodies against voltage-dependent potassium channels raised using .alpha.-dendrotoxin acceptors purified from bovine brainBiochemistry, 1992
- Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNAScience, 1992
- Alpha-dendrotoxin acceptor from bovine brain is a K+ channel protein. Evidence from the N-terminal sequence of its larger subunitJournal of Biological Chemistry, 1990
- Dendrotoxin acceptor from bovine synaptic plasma membranes. Binding properties, purification and subunit composition of a putative constituent of certain voltage-activated K+ channelsBiochemical Journal, 1989
- Properties of Single K+ and Cl− Channels in Asclepias tuberosa ProtoplastsPlant Physiology, 1987
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982