Structural features of the two-component system LisR/LisK suggests multiple responses for the adaptation and survival of Listeria monocytogenes
| Autor: | Edgar Antonio Reyes Montaño, Myriam Sánchez-Gómez, Andrés Gutiérrez Escobar, Luz Mary Salazar, Nelson Arenas Suarez |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Multidisciplinary
biology Membrana ATPase Autophosphorylation Histidine kinase LisR/LisK Two-component regulatory systems Estructura celular Listeria monocytogenes Two-component regulatory system Cell membrane medicine.anatomical_structure Biochemistry Cytoplasm Protein histidine kinase Proteínas medicine biology.protein HAMP histidina-kinasa lcsh:Science (General) Receptor lcsh:Q1-390 |
| Zdroj: | Repositorio Institucional UDCA Universidad de Ciencias Aplicadas y Ambientales U.D.C.A instacron:Universidad de Ciencias Aplicadas y Ambientales U.D.C.A Universitas Scientiarum, Vol 18, Iss 2, Pp 189-202 (2013) |
| Popis: | 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 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|