Abstract
OLE RNA is characterized by its ornate structure, large size, and distribution in anaerobic, extremophilic Gram‐positive bacteria. All organisms that carry OLE express a membrane‐spanning protein of unknown function, termed OLE‐Associated Protein (OAP). Through gel shift assays, we have demonstrated that Bacillus halodurans OLE and OAP form a specific ribonucleoprotein complex and isolated the probable binding site within the OLE molecule. We used RNA fluorescence in situ hybridization (RNA FISH) to visualize the location of OLE within the cell. In Escherichia coli cells carrying transgenic OLE and OAP, OLE is localized to the membrane only when OAP is co‐expressed. Northern blot analysis of B. halodurans shows that OLE is upregulated in the presence of the membrane stressor ethanol. Additionally, high‐throughput sequencing of wild‐type and OLE/OAP knockouts of B. halodurans reveals that OLE is extremely abundant in cells, and that lack of either OLE or OAP causes an upregulation in specific energy‐generating pathways. Together, these results suggest that OLE is involved in a function associated with membrane biochemistry. This research was supported by the Howard Hughes Medical Institute.
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