Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment
Haber-Pohlmeier S, Abarca-Heidemann K, Koerschen HG, Dhiman HK, Heberle J, Schwalbe H, Klein-Seetharaman J, Kaupp UB, Pohlmeier A (2007)
BIOPHYSICAL JOURNAL 92(9): 3207-3214.
Zeitschriftenaufsatz
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Autor*in
Haber-Pohlmeier, S.;
Abarca-Heidemann, K.;
Koerschen, H. G.;
Dhiman, H. Kaur;
Heberle, J.;
Schwalbe, H.;
Klein-Seetharaman, J.;
Kaupp, U. B.;
Pohlmeier, A.
Abstract / Bemerkung
Rod photoreceptors contain three different glutamic acid-rich proteins (GARPs) that have been proposed to control the propagation of Ca2+ from the site of its entry at the cyclic nucleotide-gated channel to the cytosol of the outer segment. We tested this hypothesis by measuring the binding of Ca2+ to the following five constructs related to GARPs of rod photoreceptors: a 32-mer peptide containing 22 carboxylate groups, polyglutamic acid, a recombinant segment comprising 73 carboxylate groups (GLU), GARP1, and GARP2. Ca2+ binding was investigated by means of a Ca2+-sensitive electrode. In all cases, Ca2+ binds with low affinity; the half-maximum binding constant K-1/2 ranges from 6 to 16 mM. The binding stoichiometry between Ca2+ ions and carboxylic groups is; 1:1; an exception is GARP2, where a binding stoichiometry of; 1:2 was found. Hydrodynamic radii of 1.6, 2.8, 3.3, 5.7, and 6.7 nm were determined by dynamic light scattering for the 32-mer, polyglutamic acid, GLU, GARP2, and GARP1 constructs, respectively. These results suggest that the peptides as well as GARP1 and GARP2 do not adopt compact globular structures. We conclude that the structures should be regarded as loose coils with low-affinity, high-capacity Ca2+ binding.
Erscheinungsjahr
2007
Zeitschriftentitel
BIOPHYSICAL JOURNAL
Band
92
Ausgabe
9
Seite(n)
3207-3214
ISSN
0006-3495
Page URI
https://pub.uni-bielefeld.de/record/1594846
Zitieren
Haber-Pohlmeier S, Abarca-Heidemann K, Koerschen HG, et al. Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment. BIOPHYSICAL JOURNAL. 2007;92(9):3207-3214.
Haber-Pohlmeier, S., Abarca-Heidemann, K., Koerschen, H. G., Dhiman, H. K., Heberle, J., Schwalbe, H., Klein-Seetharaman, J., et al. (2007). Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment. BIOPHYSICAL JOURNAL, 92(9), 3207-3214. https://doi.org/10.1529/biophysj.106.094847
Haber-Pohlmeier, S., Abarca-Heidemann, K., Koerschen, H. G., Dhiman, H. Kaur, Heberle, J., Schwalbe, H., Klein-Seetharaman, J., Kaupp, U. B., and Pohlmeier, A. 2007. “Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment”. BIOPHYSICAL JOURNAL 92 (9): 3207-3214.
Haber-Pohlmeier, S., Abarca-Heidemann, K., Koerschen, H. G., Dhiman, H. K., Heberle, J., Schwalbe, H., Klein-Seetharaman, J., Kaupp, U. B., and Pohlmeier, A. (2007). Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment. BIOPHYSICAL JOURNAL 92, 3207-3214.
Haber-Pohlmeier, S., et al., 2007. Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment. BIOPHYSICAL JOURNAL, 92(9), p 3207-3214.
S. Haber-Pohlmeier, et al., “Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment”, BIOPHYSICAL JOURNAL, vol. 92, 2007, pp. 3207-3214.
Haber-Pohlmeier, S., Abarca-Heidemann, K., Koerschen, H.G., Dhiman, H.K., Heberle, J., Schwalbe, H., Klein-Seetharaman, J., Kaupp, U.B., Pohlmeier, A.: Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment. BIOPHYSICAL JOURNAL. 92, 3207-3214 (2007).
Haber-Pohlmeier, S., Abarca-Heidemann, K., Koerschen, H. G., Dhiman, H. Kaur, Heberle, J., Schwalbe, H., Klein-Seetharaman, J., Kaupp, U. B., and Pohlmeier, A. “Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment”. BIOPHYSICAL JOURNAL 92.9 (2007): 3207-3214.
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