Characterization of the bacillus subtilis response to changes in temperature by the activity of the enzyme desaturase [delta]-5 des

Lipids provide the ideal matrix and the right physical conditions for many proteins that are in charge of many cellualr functions. However, lipid membranes not only represent the scenario on which cellular functions are carried out, it has also been argued that lipids play an active role in biochemical membrane processes. For this reason, the appropriate physical conditions are required in order to maintain the ideal physiological state of the cells. In this study, the changes in lipid chain order during cold shock in the bacterium Bacillus subtilis were studied by means of the quantification of Generalized Polarization (GP) using the fluorescent probe di-4-ANEPPDHQ in vivo and the expression levels of the desaturase [delta]-5 des (as GFP fluorescence) were measured to determine its role as the primary response mechanism to restore membrane fluidity when temperaure is lowered. The data obtained from the GP quantification presented high levels of noise, but a recovery in membrane fluidity was discernible. This result appeared approximately at the time when the GFP levels peaked, showing that the lipid chain modification might be a consequence of [delta]-5 des activity. Additionally, the fusion of the [delta]-5 des promoter with the Enhanced Cyan Fluorescent Protein (ECFP) coding sequence modified with an LVA tail for rapid degradation of the protein was cloned in a vector that enables ectopic integration of the sequence in the chromosome...

• Autores: Lara Gutiérrez, Juanita María
• Tipo de recurso: Trabajo de grado de pregrado
• Fecha de publicación: 2014
• Institución: Universidad de los Andes
• Repositorio: Séneca: repositorio Uniandes
• Idioma: eng
• OAI Identifier: oai:repositorio.uniandes.edu.co:1992/62103
• Acceso en línea: http://hdl.handle.net/1992/62103
• Palabra clave: Bacillus subtilis; Lípidos; Biología
• Rights: openAccess
• License: Atribución-CompartirIgual 4.0 Internacional