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  Characterisation of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana

Köhler, C., & Neuhaus, G. (2000). Characterisation of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana. FEBS Letters, 471(2-3), 133-136. doi:10.1016/s0014-5793(00)01383-1.

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Genre: Journal Article
Alternative Title : FEBS Letters

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 Creators:
Köhler, C.1, Author           
Neuhaus, Gunther2, Author
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1External Organizations, ou_persistent22              
2external, ou_persistent22              

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Free keywords: Cyclic nucleotide-gated ion channel, Calmodulin binding site, Non-radioactive calmodulin overlay assay, Calmodulin isoform, Two-hybrid assay, Arabidopsis thaliana
 Abstract: The recently identified cyclic nucleotide-gated ion channels (AtCNGCs) from Arabidopsis thaliana have the ability to bind calmodulin. Using two different methods, we mapped the binding site of AtCNGC1 to the last predicted α helix of the cyclic nucleotide binding domain. This is in contrast to CNGCs from animals, where the calmodulin binding site is located in the N-terminus, implying that different mechanisms for CNGC modulation have evolved in animals and plants. Furthermore, we demonstrate that AtCNGC1 and AtCNGC2 have different calmodulin binding affinities and we provide evidence for target specificities among calmodulin isoforms.

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Language(s): eng - English
 Dates: 2000-04
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 471 (2-3) Sequence Number: - Start / End Page: 133 - 136 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501