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| DOI | 10.1371/JOURNAL.PONE.0185707 | ||||
| Año | 2017 | ||||
| Tipo | artículo de investigación |
Citas Totales
Autores Afiliación Chile
Instituciones Chile
% Participación
Internacional
Autores
Afiliación Extranjera
Instituciones
Extranjeras
Cytokinesis is the last stage in the cell cycle. In prokaryotes, the protein FtsZ guides cell constriction by assembling into a contractile ring-shaped structure termed the Z-ring. Constriction of the Z-ring is driven by the GTPase activity of FtsZ that overcomes the energetic barrier between two protein conformations having different propensities to assemble into polymers. FtsZ is found in psychrophilic, mesophilic and thermophilic organisms thereby functioning at temperatures ranging from subzero to >100 degrees C. To gain insight into the functional adaptations enabling assembly of FtsZ in distinct environmental conditions, we analyzed the energetics of FtsZ function from mesophilic Escherichia coli in comparison with FtsZ from thermophilic Methanocaldococcus jannaschii. Presumably, the assembly may be similarly modulated by temperature for both FtsZ orthologs. The temperature dependence of the first-order rates of nucleotide hydrolysis and of polymer disassembly, indicated an entropy-driven destabilization of the FtsZ-GTP intermediate. This destabilization was true for both mesophilic and thermophilic FtsZ, reflecting a conserved mechanism of disassembly. From the temperature dependence of the critical concentrations for polymerization, we detected a change of opposite sign in the heat capacity, that was partially explained by the specific changes in the solvent-accessible surface area between the free and polymerized states of FtsZ. At the physiological temperature, the assembly of both FtsZ orthologs was found to be driven by a small positive entropy. In contrast, the assembly occurred with a negative enthalpy for mesophilic FtsZ and with a positive enthalpy for thermophilic FtsZ. Notably, the assembly of both FtsZ orthologs is characterized by a critical concentration of similar value (1-2 mu M) at the environmental temperatures of their host organisms. These findings suggest a simple but robust mechanism of adaptation of FtsZ, previously shown for eukaryotic tubulin, by adjustment of the critical concentration for polymerization.
| Ord. | Autor | Género | Institución - País |
|---|---|---|---|
| 1 | CONCHA-MARAMBIO, LUIS MIGUEL | Hombre |
Universidad de Chile - Chile
Ampr Inc - Estados Unidos Amprion Inc. - Estados Unidos |
| 2 | MALDONADO-MALDONADO, PAULA | Mujer |
Universidad de Chile - Chile
Francis Crick Inst - Reino Unido The Francis Crick Institute - Reino Unido |
| 3 | LAGOS-MONACO, ROSALBA LUCIA | Mujer |
Universidad de Chile - Chile
|
| 4 | MONASTERIO-OPAZO, OCTAVIO HERNAN | Hombre |
Universidad de Chile - Chile
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| 5 | Montecinos-Franjola, Felipe | Hombre |
Universidad de Chile - Chile
Eunice Kennedy Shriver Natl Inst Child Hlth & Hum - Estados Unidos National Institute of Child Health and Human Development - Estados Unidos National Institute of Child Health and Human Development (NICHD) - Estados Unidos |
| Fuente |
|---|
| Fondo Nacional de Desarrollo Científico y Tecnológico |
| Comisión Nacional de Investigación Científica y Tecnológica |
| Becas Chile and Programa de Mejoramiento de la Calidad y Equidad de la Educacion |
| Agradecimiento |
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| FMF received funding from Becas Chile and Programa de Mejoramiento de la Calidad y Equidad de la Educacion, and was supported by Comision Nacional de Investigacion Cientifica y Tecnologica grant 24090139. OM received financial support from Fondo Nacional de Desarrollo Cientifico y Tecnologico grant 1130711. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. |