Calcium-dependent structural changes in human reticulocalbin-1.
2014
: Human reticulocalbin-1 (hRCN1) has six EF-hand motifs and binds Ca(2+). hRCN1 is a member of the CREC family localized in the secretory pathway, and its cellular function remains unclear. In this study, we established a new bacterial expression and purification procedure for hRCN1. We observed that hRCN1 binds Ca(2+) in a cooperative manner and the Ca(2+) binding caused an increase in the α-helix content of hRCN1. On the other hand, hRCN1 did not change the structure with Mg(2+) loading. hRCN1 is a monomeric protein, and its overall structure became more compact upon Ca(2+) binding, as revealed by gel-filtration column chromatography and small-angle X-ray scattering. This is the first report of conformational changes in the CREC family upon Ca(2+) binding. Our data suggest that CREC family member interactions with target proteins are regulated in the secretory pathway by conformational changes upon Ca(2+) binding.
Keywords:
- Calcium
- Helix (Snails)
- Biophysics
- Diagnostic radiologic examination
- Reticulocalbin 1
- Secretory pathway
- Crystallography
- EF-Hand Motif
- Edetate disodium
- Biochemistry
- Chemistry
- Binding (Molecular Function)
- Small-angle X-ray scattering
- Column chromatography
- Chromatography column
- Proteolysis
- Gel permeation chromatography
- Correction
- Source
- Cite
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