Vol. 18 No. 2 (2013), Bioinformatics and modeling
Vol. 18 No. 2 (2013)

Structural features of the two-component system LisR/LisK suggests multiple responses for the adaptation and survival of Listeria monocytogenes

Bioinformatics and modeling
Published 2013-08-26
Nelson Arenas Suarez
Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, Denmark
Andrés Gutiérrez Escobar
Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.
Myriam Sánchez-Goméz
Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Luz Mary Salazar
Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Edgar Reyes Montaño
Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
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Keywords

Listeria monocytogenes
LisR/LisK
two-component regulatory systems
protein histidine kinase.

How to Cite

Structural features of the two-component system LisR/LisK suggests multiple responses for the adaptation and survival of Listeria monocytogenes. (2013). Universitas Scientiarum, 18(2), 189-202. https://doi.org/10.11144/Javeriana.SC18-2.sfts
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Abstract

Here, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the cell membrane and its modular composition (HAMP, histidine kinase and ATPase domains) is associated with its autophosphorylation (His-266). A stimulus-response likely determines the sequential signal propagation from the bacterial cell surface to its cytoplasmic components. According to our results, LisR is a cytoplasmic protein with a receptor domain (homologous to CheY) that comprises a phosphoacceptor residue (Asp-52) and a DNA-binding domain, which may allow the transmission of a specific transcriptional response. LisR/LisK has been experimentally characterized both biochemically and functionally in other Bacilli pathophysiology; our structure-function approach may facilitate the design of suitable inhibitors.

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