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Two distinct calcium‐calmodulin interactions with N‐terminal regions of the olfactory and rod cyclic nucleotide‐gated channels characterized by NMR spectroscopy
Author(s) -
Orsale Maria,
Melino Sonia,
Contessa Gian Marco,
Torre Vincent,
Andreotti Giuseppina,
Motta Andrea,
Paci Maurizio,
Desideri Alessandro,
Cicero Daniel O
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00716-6
Subject(s) - calmodulin , cyclic nucleotide gated ion channel , protein subunit , nucleotide , chemistry , biophysics , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , cyclic nucleotide , biochemistry , biology , enzyme , gene
The interactions of calcium‐calmodulin with two fragments of the N‐terminal domains of the olfactory α‐subunit and rod β‐subunit cyclic nucleotide‐gated channels have been investigated using nuclear magnetic resonance spectroscopy. The results indicate that in the two cases both the N‐terminal and the C‐terminal calmodulin lobes are involved in the interaction. The olfactory cyclic nucleotide‐gated channel segment forms a 1:1 complex with calmodulin, whereas the rod fragment forms a 2:1 complex. The correlation times of the two complexes, as estimated by 15 N relaxation studies, are compatible with the observed stoichiometries. These results indicate differences in the mode of action by which calmodulin modulates the activity of both channels, and suggest either that the rod channel is modulated through a simultaneous interaction of two β‐subunits with calmodulin or that other regions of the N‐terminus are necessarily implicated in the binding.