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.

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Abstract
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.
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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.
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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25 References

Data provided by Europe PubMed Central.

Cyclic nucleotide-gated ion channels.
Kaupp UB, Seifert R., Physiol. Rev. 82(3), 2002
PMID: 12087135
A 240 kDa protein represents the complete beta subunit of the cyclic nucleotide-gated channel from rod photoreceptor.
Korschen HG, Illing M, Seifert R, Sesti F, Williams A, Gotzes S, Colville C, Muller F, Dose A, Godde M., Neuron 15(3), 1995
PMID: 7546742
Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.
Korschen HG, Beyermann M, Muller F, Heck M, Vantler M, Koch KW, Kellner R, Wolfrum U, Bode C, Hofmann KP, Kaupp UB., Nature 400(6746), 1999
PMID: 10466724

AUTHOR UNKNOWN, 1960

AUTHOR UNKNOWN, 1977
Glutamic acid-rich proteins of rod photoreceptors are natively unfolded.
Batra-Safferling R, Abarca-Heidemann K, Korschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB., J. Biol. Chem. 281(3), 2006
PMID: 16280326
Intrinsically unstructured proteins and their functions.
Dyson HJ, Wright PE., Nat. Rev. Mol. Cell Biol. 6(3), 2005
PMID: 15738986
Intrinsically unstructured proteins.
Tompa P., Trends Biochem. Sci. 27(10), 2002
PMID: 12368089

AUTHOR UNKNOWN, 1990

AUTHOR UNKNOWN, 1982

AUTHOR UNKNOWN, 1982

AUTHOR UNKNOWN, 2004

AUTHOR UNKNOWN, 2002

AUTHOR UNKNOWN, 2001

AUTHOR UNKNOWN, 1980

AUTHOR UNKNOWN, 1990
High-affinity and low-affinity calcium binding and stability of the multidomain extracellular 40-kDa basement membrane glycoprotein (BM-40/SPARC/osteonectin).
Maurer P, Mayer U, Bruch M, Jeno P, Mann K, Landwehr R, Engel J, Timpl R., Eur. J. Biochem. 205(1), 1992
PMID: 1555584
Ca2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin.
Mitchell RD, Simmerman HK, Jones LR., J. Biol. Chem. 263(3), 1988
PMID: 3335548
Counterion condensation revisited.
Manning GS, Ray J., J. Biomol. Struct. Dyn. 16(2), 1998
PMID: 9833682
Impaired channel targeting and retinal degeneration in mice lacking the cyclic nucleotide-gated channel subunit CNGB1.
Huttl S, Michalakis S, Seeliger M, Luo DG, Acar N, Geiger H, Hudl K, Mader R, Haverkamp S, Moser M, Pfeifer A, Gerstner A, Yau KW, Biel M., J. Neurosci. 25(1), 2005
PMID: 15634774

AUTHOR UNKNOWN, 2003

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