Premium
New insights into the interaction between the quorum‐sensing receptor NprR and its DNA target, or the response regulator Spo0F
Author(s) -
Cabrera Rosina,
RodríguezRomero Adela,
Guarneros Gabriel,
Torre Mayra
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12371
Subject(s) - quorum sensing , biology , function (biology) , dna , microbiology and biotechnology , plasma protein binding , response regulator , regulator , biochemistry , bacteria , genetics , bacterial protein , gene , virulence
The NprR protein and Npr RB 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 Npr RB signaling peptide SSKPDIVG that binds strongly to Apo‐NprR, failed to bind and disrupt the NprR‐Spo0F complex. Finally, the NprR‐Npr RB 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 Npr RB , the NprR/Npr RB ratio and the availability of Spo0F binding sites define the function of NprR.