Proteomics

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Identification of RNA chaperones by gradient profiling in the Lyme disease spirochete, Borrelia burgdorferi


ABSTRACT: RNA-binding proteins (RBPs) play key roles in regulating gene expression in bacteria. However, relatively few RBPs have been discovered and characterized in Borrelia (Borreliella) burgdorferi, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. We employed in vitro and in vivo assays to characterize the RNA chaperone activities of several proteins we identified in the gradient profiling. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and the flagella-associated protein FlgV displayed dramatic RNA annealing and/or strand displacement activity. Moreover, in vivo Co-IP assays demonstrated BB0749 binds RNA in B. burgdorferi.

INSTRUMENT(S):

ORGANISM(S): Borreliella Burgdorferi

TISSUE(S): Blood Cell

DISEASE(S): Lyme Disease

SUBMITTER: Christopher Ebmeier  

LAB HEAD: Meghan Lybecker

PROVIDER: PXD068462 | Pride | 2026-06-29

REPOSITORIES: Pride

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Publications

Identification of proteins exhibiting <i>in vitro</i> RNA chaperone activity through gradient profiling in the Lyme disease spirochete, <i>Borrelia burgdorferi</i>.

Van Gundy Taylor T   Schneider Cornelius C   Ebmeier Christopher C CC   Chambers Gavin Z GZ   Cramer Nicholas A NA   Chambers Kathryn Mf KM   Drecktrah Dan D   Hyde Jenny A JA   Skare Jon T JT   Marconi Richard T RT   Samuels D Scott DS   Lybecker Meghan C MC  

RNA biology 20260618 1


RNA-binding proteins (RBPs) play key roles in regulating gene expression across all domains of life. However, relatively few RBPs have been discovered and characterized in <i>Borrelia</i> (<i>Borreliella</i>) <i>burgdorferi</i>, the causative agent of Lyme disease. We utilized gradient profiling to identify putative RBPs that co-sediment with small RNAs (sRNAs) and nascent mRNAs. The previously hypothetical proteins BB0749, BB0713 and BB0796, as well as the chemotaxis-related protein CheY2 and t  ...[more]

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