MassIVE MSV000094854

Partial Public PXD052534

Using MS2 affinity pulldown to identify sRNA associating proteins in the bacterium Deinococcus radiodurans

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Description

We carried out the widely used MS2 aptamer approach to identify the proteins that could potentially interact with sRNAs in D. radiodurans. The MS2 aptamer was fused to the 5 extremity of PprS/Dsr2, a well-characterized D. radiodurans sRNA . This construct is then expressed off the pRADgro plasmid in wild-type D. radiodurans at mid-exponential phase. After bacterial lysis, the crude extract was loaded into an amylose-based chromatography column previously coated with the MS2 protein fused to the maltose-binding protein. This enables the specific capture of MS2-Dsr2 and its interacting protein partners. After elution, co-purified proteins were identified by LC-MS/MS and subsequent bioinformatic analysis [doi:10.25345/C52J68G3Z] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: small RNA ; RNA-protein interaction ; RNA binding protein ; RNA regulation ; Deinococcus radiodurans

Contact

Principal Investigators:
(in alphabetical order) 		Lydia M. Contreras, the University of Texas at Austin, United States
Submitting User: Runhuahan
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