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Identifying Protein-Protein Interactions of DDX41 by BioID

Date

2022

Authors

Toliat Zavareh, Seyed Mohammad Mahdi
Charaya, Ananaya
Xiang, Jim
Wu, Yuliang

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Poster Presentation

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Abstract

Helicases are known as enzymes that separate double-stranded(ds) nucleic acids to single-strand(ss) nucleic acids by hydrolysis ATP; and some of them also can anneal ss nucleic acids to ds nucleic acids in an ATP-independent manner. DEAD-box helicases are characterized by containing an Asp-Glu-Ala-Asp (DEAD) sequence in their motif II that is required for ATP binding and hydrolysis. DEAD-box helicase 41 (DDX41) is a member of DEAD-box helicases with multiple functions, including acting as a sensor for intracellular DNA in myeloid dendritic cells1 and for bacterial secondary messengers (c-di-GMP or c-di-AMP) to trigger type 1 interferon production2. Recently, the Dr. Wu’s lab discovered that DDX41 modulates the balance of dsDNA and ssDNA, in which regulates the activation of the cyclic GMP–AMP synthase (cGAS)3. Mutations in DDX41 are linked with myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML)4, two blood caners. The most recurring mutation in DDX41 that lead to AML or MDS is c.1574G>A (p.R525H). Despite concrete evidence suggests that DDX41 acts as a DNA sensor in innate immunity5,6; no innate immunity-related protein has been identified as a DDX41-binding partner. Therefore, we established a BioID system to identify DDX41-biniding proteins under virus infections.

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Keywords

protein-protein interactions, DDX41

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