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Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein

dc.contributor.authorPáez Pérez, Edgar Daniel
dc.contributor.authorBenítez Cardoza, Claudia Guadalupe
dc.contributor.authorMontero Morán, Gabriela Margarita
dc.contributor.authorLara González, Samuel
dc.identifier.citationACS Omega 2020, 5, 40, 25841-25847 Publication Date:October 5, 2020 Copyright © 2020 American Chemical Society
dc.description.abstract"G0S2 is a small protein of 103 residues in length that is involved in multiple cellular processes. To date, several reports have shown that G0S2 functions by making direct protein杙rotein interactions with key proteins. In lipolysis, G0S2 specifically interacts with adipose triglyceride lipase, inhibiting its activity and resulting in lipolysis being downregulated. In a similar way, G0S2 also participates in the regulation of apoptosis, cell proliferation, and oxidative phosphorylation; however, information regarding G0S2 structural and biophysical properties is limited. In this work, we conducted a comparative structural analysis of human and mouse G0S2 proteins. Bioinformatics suggests the presence of a disordered C-terminal region in human G0S2. Experimental characterization by size-exclusion chromatography and dynamic light scattering showed that human and mouse G0S2 have different hydrodynamic properties. In comparison to the mouse G0S2, which behaves similar to a globular protein, the human G0S2 shows an elongated conformation, most likely by displaying a disordered C-terminal region. Further analysis of hydrodynamic properties under denaturing conditions suggests the presence of a structural element in the mouse protein that undergoes an order to disorder transition at low urea concentration. Structural analysis by circular dichroism revealed that in native conditions, both proteins are mainly unstructured, showing the presence of beta sheet structures. Further analysis of CD data suggests that both proteins belong to the premolten globule family of intrinsically disordered proteins. We suggest that the intrinsic disorder observed in the G0S2 protein may facilitate its interaction with multiple partners in the regulation of cellular metabolism."
dc.publisherAmerican Chemical Society
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.subjectG0/G1 Switch Gene
dc.titleBioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein
dc.rights.accessAcceso Abierto

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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 Internacional