Mechanistic Insights into Chromatin Recognition by the SAND Domain of Speckled Protein 110C
Lathrop, Annika
Lathrop, Annika
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Abstract
Speckled proteins (SP) are chromatin-binding proteins that transcriptionally regulate gene silencing in immune cells. Mutations within SPs are correlated with immunodeficiency, inflammation, and viral disease. SP110C is expressed in innate and adaptive immune cells as well as non-immune cells and is essential for adaptive immune cell development and function. Loss of function mutations in SP110 are associated with an immunodeficiency of the adaptive immune system. SP110 contains several functional domains that drive the protein�s activity, including a conserved SAND domain that is hypothesized to interact with DNA in several proteins linked to disease. However, the structure, function, and molecular interactions that drive the SAND domain�s activity have remained uncharacterized in SP110C. Diffraction Light Scattering and chromatographic analysis prove that the SAND domain likely dimerizes in solution, and the SAND domain is now shown to be sufficient to mediate DNA binding in SP110C. Specifically the K512, N513, and R516 residues are critical to facilitate binding. This functional characterization indicates that SP110 SAND domain may be an effective target for reducing cellular inflammation and viral infection.
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Date
1/1/2026
Student Status
Senior (Graduating in 2026)
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Oral Presentation
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Biochemistry
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College of Arts and Sciences
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Life Science