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FEBS Lett. 2016 Sep;590(18):3243-53. doi: 10.1002/1873-3468.12371. Epub 2016 Sep 2.

New insights into the interaction between the quorum-sensing receptor NprR and its DNA target, or the response regulator Spo0F.

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Centro de Investigación en Alimentación y Desarrollo A. C., Hermosillo, Mexico.
Instituto de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, Ciudad de México, México.
Departamento de Genética y Biología Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Ciudad de México, México.
Centro de Investigación en Alimentación y Desarrollo A. C., Hermosillo, Mexico.


The NprR protein and NprRB signaling peptide comprise a bifunctional quorum-sensing system from the Bacillus cereus group that is involved in transcriptional activation through DNA-binding and in sporulation initiation by binding to Spo0F. We characterized in vitro the direct interactions established by NprR that may be relevant for performing its two functions. Apo-NprR interacted with Spo0F, but not with the target DNA. The NprRB signaling peptide SSKPDIVG that binds strongly to Apo-NprR, failed to bind and disrupt the NprR-Spo0F complex. Finally, the NprR-NprRB complex bound both to Spo0F and the target DNA with similar affinity. Based on our findings, we propose that rather than a switch triggered by NprRB, the NprR/NprRB ratio and the availability of Spo0F binding sites define the function of NprR.


NprR; NprR-Spo0F interaction; bifunctional quorum-sensing regulator

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