TY  - JOUR
AU  - Cukkemane, A.
AU  - Grüter, B.
AU  - Novak, K.
AU  - Gensch, T.
AU  - Bönigk, W.
AU  - Gerharz, T.
AU  - Kaupp, U. B.
AU  - Seifert, R.
TI  - Subunits act independently in a cyclic nucleotide-activated K+ channel
JO  - EMBO reports
VL  - 8
SN  - 1469-221X
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - PreJuSER-57477
SP  - 749 - 755
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - Ion channels gated by cyclic nucleotides have crucial roles in neuronal excitability and signal transduction of sensory neurons. Here, we studied ligand binding of a cyclic nucleotide-activated K(+) channel from Mesorhizobium loti and its isolated cyclic nucleotide-binding domain. The channel and the binding domain alone bind cyclic AMP with similar affinity in a non-cooperative manner. The cAMP sensitivities of binding and activation coincide. Thus, each subunit in the tetrameric channel acts independently of the others. The binding and gating properties of the bacterial channel are distinctively different from those of eukaryotic cyclic nucleotide-gated channels.
KW  - Alphaproteobacteria: metabolism
KW  - Bacterial Proteins: chemistry
KW  - Bacterial Proteins: genetics
KW  - Cyclic AMP: chemistry
KW  - Cyclic Nucleotide-Gated Cation Channels: chemistry
KW  - Cyclic Nucleotide-Gated Cation Channels: genetics
KW  - Ligands
KW  - Potassium Channels: chemistry
KW  - Potassium Channels: genetics
KW  - Protein Structure, Tertiary
KW  - Protein Subunits: chemistry
KW  - Spectrometry, Fluorescence
KW  - Bacterial Proteins (NLM Chemicals)
KW  - Cyclic Nucleotide-Gated Cation Channels (NLM Chemicals)
KW  - Ligands (NLM Chemicals)
KW  - Potassium Channels (NLM Chemicals)
KW  - Protein Subunits (NLM Chemicals)
KW  - Cyclic AMP (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17668006
C2  - pmc:PMC1978089
UR  - <Go to ISI:>//WOS:000248447300011
DO  - DOI:10.1038/sj.embor.7401025
UR  - https://juser.fz-juelich.de/record/57477
ER  -