IDIM   12530
INSTITUTO DE INVESTIGACIONES MEDICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
ClpX2 REGULATES NifB AND NifEN LEVELS DURING
Autor/es:
MARTÍNEZ-NOËL G; CURATTI L; HERNANDEZ J; RUBIO L
Lugar:
Puerto Madryn
Reunión:
Congreso; SAIB; 2010
Institución organizadora:
SAIB
Resumen:
Biological nitrogen fixation is mainly catalyzed by the molybdenum
nitrogenase that carries at its active site the iron and molybdenum
cofactor (FeMo-co). Among the genes that are required for the
biosynthesis of FeMo-co nifB is remarkable because it is also
essential for the biosyntheses of the cofactors all alternative
nitrogenases. In this work, we show evidence suggesting the
operation of a nitrogen source-dependent mechanism for the
degradation of NifB and NifEN in A. vinelandii and that a duplicated
copy of the ATPase component of the ClpXP protease (ClpX2) is
involved in this regulatory pathway. clpX2 was induced under
nitrogen fixing conditions and its inactivation slow-down NifB
turnover and resulted in the accumulation of NifB and NifEN. clpX2
mutants displayed a defect in diazotrophic growth, especially when
iron was limiting. Inactivation of other genes related to NifB activity
(nifENX) also affected NifB degradation rates suggesting that NifB
susceptibility to degradation might change during its catalytic cycle.
ANPCyT.