Bacillus subtilis SalA is a phosphorylation-dependent transcription regulator that represses scoC and activates the production of the exoprotease AprE.
2015
Derouiche, Abderahmane | Shi, Lei | Bidnenko, Vladimir | Ventroux, Magali | Pigonneau, Nathalie | Franz-Wachtel, Mirita | Kalantari, Aida | Nessler, Sylvie | Noirot-Gros, Marie-Françoise | Mijakovic, Ivan | Systems and Synthetic Biology, Department of Chemical and Biological Engineering ; Chalmers University of Technology [Göteborg] | MICrobiologie de l'ALImentation au Service de la Santé (MICALIS) ; Institut National de la Recherche Agronomique (INRA)-AgroParisTech | Proteome Center ; Eberhard Karls Universität Tübingen = University of Tübingen | We thank Dina Petranovic for valuable discussions and critical reading of the manuscript, Fredrik Westerlund for assistance with circular dichroism measurements and Silke Wahl and Johannes Madlung for excellent technical support.This work was supported by the Agence Nationale de la Recherche (2010-BLAN-1303-01) (to IM, MFNG and SN), and Chalmers University of Technology (to IM).
Il y a une coquille sur le nom de famille d'un des auteurs. Il faut lire Nathalie Pigeonneau et non Nathalie Pigonneau.
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Mostrar más [+] Menos [-]Inglés. Bacillus subtilis Mrp family protein SalA has been shown to indirectly promote the production of the exoprotease AprE by inhibiting the expression of scoC, which codes for a repressor of aprE. The exact mechanism by which SalA influences scoC expression has not been clarified previously. We demonstrate that SalA possesses a DNA-binding domain (residues 1-60), which binds to the promoter region of scoC. The binding of SalA to its target DNA depends on the presence of ATP and is stimulated by phosphorylation of SalA at tyrosine 327. The B. subtilis protein-tyrosine kinase PtkA interacts specifically with the C-terminal domain of SalA in vivo and in vitro and is responsible for activating its DNA binding via phosphorylation of tyrosine 327. In vivo, a mutant mimicking phosphorylation of SalA (SalA Y327E) exhibited a strong repression of scoC and consequently overproduction of AprE. By contrast, the non-phosphorylatable SalA Y327F and the ΔptkA exhibited the opposite effect, stronger expression of scoC and lower production of the exoprotease. Interestingly, both SalA and PtkA contain the same ATP-binding Walker domain and have thus presumably arisen from the common ancestral protein. Their regulatory interplay seems to be conserved in other bacteria.
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