Oliveras Cabrera, Adriana

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    The effects of centrin mutations on the affinity, stability, and structure of the Centrin-Sfi1p21 complex
    (2018) Oliveras Cabrera, Adriana; Pastrana Ríos, Belinda; College of Arts and Sciences - Sciences; Guzmán Martínez, Aikomarí; Ríos Steiner, Jorge; Department of Chemistry; Velazquez Figueroa, Carlos
    Centrin is a small, calcium binding protein part of the EF-hand superfamily. As one of the 347 eukaryotic signature proteins (ESPs), centrin has no bacterial or archaea homologue. Centrin is required for centriole duplication and assembly of cilia and flagella. In human cells, centrin is found as three isoforms, termed centrin 1-3, respectively. Centrin 1 is found in the base of the flagella in the sperm, centrin 2 and centrin 3 are ubiquitously expressed in all somatic cells, but centrin 2 has also been found to regulate DNA excision repair within the nucleus and export mRNA and other proteins from the nucleus. As an ESP, centrin has a wide range of biological targets with whom it interacts, one of them being Sfi1. Sfi1 is a vital centriolar protein required for its duplication. Variations in centrin’s sequence can affect its structure and function, resulting in weaker interactions with its biological targets. Circular dichroism (CD) and isothermal titration calorimetry (ITC) are spectroscopic and thermodynamic techniques, respectively, that were used to characterize non-conserved mutations in centrin 1 and centrin 2 and their effect on centrin’s secondary structure and its interaction with a fragment of human Sfi1 (HsSfi1p21). From CD analyses it was observed that the non-conserved variations contribute to the helical content and increase thermal stability. Thermodynamic binding parameters obtained by ITC indicated that the non-conserved variation affected the interaction interface between the studied variant and HsSfi1p21.