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Association of plant K+inchannels is mediated by conserved C-termini and does not affect subunit assembly

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
409
Issue
2
Identifiers
DOI: 10.1016/s0014-5793(97)00502-4
Keywords
  • Guard Cell
  • Insect Cell
  • Potassium Channel
  • Two-Hybrid System
  • Potato
Disciplines
  • Biology

Abstract

Abstract Inward rectifying potassium (K + in) channels play an important role in turgor regulation and ion uptake in higher plants. Here, we report a previously unrecognized feature of these proteins: K + in channel C-terminal polypeptides mediate channel protein interactions. Using a C-terminal fragment of potato guard cell K + in channel KST1 in a yeast two-hybrid screen two novel putative K + in channel proteins (SKT2 and SKT3) were identified by interaction of their C-termini which contained a conserved domain (K HA). Interactions were confirmed by Western blot-related assays utilizing K + in channel C-termini fused to green fluorescence protein. Although deletion of the K HA-domain abolished these interactions, K + in currents were still detectable by patch-clamp measurements of insect cells expressing these KST1 mutants, indicating that formation of a functional channel does not depend on this C-terminal domain.

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