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G-Quadruplexes Act as Sequence Dependent Chaperones via Protein Oligomerization

Adam Begeman, Theodore J. Litberg, Jennifer Bourne, Zhenyu Xuan, Scott Horowitz
doi: https://doi.org/10.1101/850263
Adam Begeman
Department of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, Colorado 80208, United States
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Theodore J. Litberg
Department of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, Colorado 80208, United States
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Jennifer Bourne
Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 80045 United States
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Zhenyu Xuan
Department of Biological Sciences, Center for Systems Biology, University of Texas at Dallas, Richardson, TX 75080, United States
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Scott Horowitz
Department of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, Colorado 80208, United States
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  • For correspondence: scott.horowitz@du.edu
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Abstract

Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent aggregation up to 300-fold more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over 500 nucleic acid sequences’ effects on aggregation, we demonstrate that the holdase chaperone effect of nucleic acids is highly sequence dependent. Quadruplexes are found to have especially potent effects on aggregation with many different proteins via quadruplex:protein oligomerization. These observations contextualize recent reports of quadruplexes playing important roles in aggregation-related diseases, such as Fragile X and Amyotrophic lateral sclerosis (ALS).

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Posted November 21, 2019.
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G-Quadruplexes Act as Sequence Dependent Chaperones via Protein Oligomerization
Adam Begeman, Theodore J. Litberg, Jennifer Bourne, Zhenyu Xuan, Scott Horowitz
bioRxiv 850263; doi: https://doi.org/10.1101/850263
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G-Quadruplexes Act as Sequence Dependent Chaperones via Protein Oligomerization
Adam Begeman, Theodore J. Litberg, Jennifer Bourne, Zhenyu Xuan, Scott Horowitz
bioRxiv 850263; doi: https://doi.org/10.1101/850263

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