Send to

Choose Destination
RNA Biol. 2016 Sep;13(9):916-26. doi: 10.1080/15476286.2016.1208894. Epub 2016 Jul 22.

Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA.

Author information

a AG Bakteriengenetik, Lehrstuhl für Genetik, Friedrich-Schiller-Universität Jena , Philosophenweg , Jena , Germany.


SR1 is a dual-function sRNA from B. subtilis that acts as a base-pairing regulatory RNA and as a peptide-encoding mRNA. Both functions of SR1 are highly conserved. Previously, we uncovered that the SR1 encoded peptide SR1P binds the glycolytic enzyme GapA resulting in stabilization of gapA mRNA. Here, we demonstrate that GapA interacts with RNases Y and J1, and this interaction was RNA-independent. About 1% of GapA molecules purified from B. subtilis carry RNase J1 and about 2% RNase Y. In contrast to the GapA/RNase Y interaction, the GapA/RNaseJ1 interaction was stronger in the presence of SR1P. GapA/SR1P-J1/Y displayed in vitro RNase activity on known RNase J1 substrates. Moreover, the RNase J1 substrate SR5 has altered half-lives in a ΔgapA strain and a Δsr1 strain, suggesting in vivo functions of the GapA/SR1P/J1 interaction. Our results demonstrate that the metabolic enzyme GapA moonlights in recruiting RNases while GapA bound SR1P promotes binding of RNase J1 and enhances its activity.


B. subtilis; GAPDH; RNase J1; RNase Y; dual function sRNA; moonlighting protein; small regulatory RNA

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center