Rapid kinetics of calcium dissociation from plant calmodulin and calmodulin-like proteins and effect of target peptides

Troilo, Francesca; Pedretti, Marco; Allocatelli, Carlo Travaglini; Astegno, Alessandra; Matteo, Adele Di

doi:10.1016/j.bbrc.2021.12.077

Cited by 4 publications

(2 citation statements)

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“…Structural studies of centrin interactions have revealed that the basis for the target selectivity of centrins lies in their ability to interact with regions that have the propensity to form an α-helix and contain a hydrophobic triad, namely W 1 xxL 4 xxxL 8 (1–4–8 motif), which can be either in a forward (W 1 L 4 L 8 ) or reverse (L 8 L 4 W 1 ) orientation [ 6 , 12 , 18 ]. This sequence has been found in many centrin–target complex structures and validated by various biophysical techniques [ 6 , 12 , 17 , 18 , 19 , 20 , 21 , 22 , 23 ].…”

Section: Introductionmentioning

confidence: 78%

“…Herein, our goal was to characterize the molecular interactions that lead to the formation of the TgCEN1-TgSFI1 complex, and the conformational changes associated with the interaction compared to the single components. We used a peptide model approach to simulate a target protein that has been employed in many studies of other Ca 2+ binding proteins and their regulatory interactions [ 8 , 12 , 18 , 20 , 23 , 47 , 48 ], and has demonstrated, in many cases, the ability to uncover crucial determinants of the interaction.…”

Section: Discussionmentioning

confidence: 99%

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Conformational Plasticity of Centrin 1 from Toxoplasma gondii in Binding to the Centrosomal Protein SFI1

et al. 2022

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Centrins are calcium (Ca2+)-binding proteins that are involved in many cellular functions including centrosome regulation. A known cellular target of centrins is SFI1, a large centrosomal protein containing multiple repeats that represent centrin-binding motifs. Recently, a protein homologous to yeast and mammalian SFI1, denominated TgSFI1, which shares SFI1-repeat organization, was shown to colocalize at centrosomes with centrin 1 from Toxoplasma gondii (TgCEN1). However, the molecular details of the interaction between TgCEN1 and TgSFI1 remain largely unknown. Herein, combining different biophysical methods, including isothermal titration calorimetry, nuclear magnetic resonance, circular dichroism, and fluorescence spectroscopy, we determined the binding properties of TgCEN1 and its individual N- and C-terminal domains to synthetic peptides derived from distinct repeats of TgSFI1. Overall, our data indicate that the repeats in TgSFI1 constitute binding sites for TgCEN1, but the binding modes of TgCEN1 to the repeats differ appreciably in terms of binding affinity, Ca2+ sensitivity, and lobe-specific interaction. These results suggest that TgCEN1 displays remarkable conformational plasticity, allowing for the distinct repeats in TgSFI1 to possess precise modes of TgCEN1 binding and regulation during Ca2+ sensing, which appears to be crucial for the dynamic association of TgCEN1 with TgSFI1 in the centrosome architecture.

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