IIB   20738
INSTITUTO DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Proteome analysis of a Lon protease mutant of the haloarchaeon Haloferax volcanii
Autor/es:
CERLETTI, M.; PAGGI, R.A.; POETSCH, A.; DE CASTRO, R.E.
Lugar:
Paris
Reunión:
Conferencia; VI Molecular Biology of Archaea Conference, Paris, Francia; 2014
Resumen:
Energy-dependent proteolysis is needed to control the quality of proteins and for the regulation of numerous cellular functions. ATP-dependent Lon proteases are ubiquitous in the three domains of Life. Within this family, Lon proteases of bacteria and eukaryotes (LonA subfamily, soluble enzymes) have been thoroughly characterized, however, the archaeal homolog (LonB subfamily, membrane-bound enzymes) has been studied to a limited extent and its relevance in archaeal physiology was known. To gain insight on the role of Lon in archaea, we previously constructed mutant strains defective in Lon expression in the model haloarchaeon Haloferax volcanii and obtained evidence indicating that this enzyme is essential for cell viability. Sub-expression of Lon resulted in cell overpigmentation,