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Identifying Protein-Protein Interactions of DDX41 by BioID

dc.contributor.authorToliat Zavareh, Seyed Mohammad Mahdi
dc.contributor.authorCharaya, Ananaya
dc.contributor.authorXiang, Jim
dc.contributor.authorWu, Yuliang
dc.date.accessioned2022-09-22T22:00:10Z
dc.date.available2022-09-22T22:00:10Z
dc.date.issued2022
dc.description.abstractHelicases 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.en_US
dc.identifier.urihttps://hdl.handle.net/10388/14205
dc.rightsAttribution-NonCommercial-ShareAlike 2.5 Canada*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/2.5/ca/*
dc.subjectprotein-protein interactionsen_US
dc.subjectDDX41en_US
dc.titleIdentifying Protein-Protein Interactions of DDX41 by BioIDen_US
dc.typePoster Presentationen_US

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