Thermodynamics of Calcium binding to the Calmodulin N-terminal domain to evaluate site-specific affinity constants and cooperativity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-06-13

AUTHORS

Maria Rosa Beccia, Sandrine Sauge-Merle, David Lemaire, Nicolas Brémond, Romain Pardoux, Stéphanie Blangy, Philippe Guilbaud, Catherine Berthomieu

ABSTRACT

Calmodulin (CaM) is an essential Ca(II)-dependent regulator of cell physiology. To understand its interaction with Ca(II) at a molecular level, it is essential to examine Ca(II) binding at each site of the protein, even if it is challenging to estimate the site-specific binding properties of the interdependent CaM-binding sites. In this study, we evaluated the site-specific Ca(II)-binding affinity of sites I and II of the N-terminal domain by combining site-directed mutagenesis and spectrofluorimetry. The mutations had very low impact on the protein structure and stability. We used these binding constants to evaluate the inter-site cooperativity energy and compared it with its lower limit value usually reported in the literature. We found that site I affinity for Ca(II) was 1.5 times that of site II and that cooperativity induced an approximately tenfold higher affinity for the second Ca(II)-binding event, as compared to the first one. We further showed that insertion of a tryptophan at position 7 of site II binding loop significantly increased site II affinity for Ca(II) and the intra-domain cooperativity. ΔH and ΔS parameters were studied by isothermal titration calorimetry for Ca(II) binding to site I, site II and to the entire N-terminal domain. They showed that calcium binding is mainly entropy driven for the first and second binding events. These findings provide molecular information on the structure–affinity relationship of the individual sites of the CaM N-terminal domain and new perspectives for the optimization of metal ion binding by mutating the EF-hand loops sequences. More... »

PAGES

905-919

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-015-1275-1

DOI

http://dx.doi.org/10.1007/s00775-015-1275-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046851677

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26070361


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67 loop sequence
68 low impact
69 lower limit value
70 metal ions
71 molecular information
72 molecular level
73 mutagenesis
74 mutations
75 new perspective
76 optimization
77 parameters
78 perspective
79 physiology
80 position 7
81 properties
82 protein
83 protein structure
84 regulator
85 relationship
86 sequence
87 site I
88 site II
89 site-directed mutagenesis
90 sites
91 spectrofluorimetry
92 stability
93 structure
94 structure-affinity relationships
95 study
96 thermodynamics
97 thermodynamics of calcium
98 time
99 titration calorimetry
100 tryptophan
101 values
102 ΔH
103 ΔS parameters
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