IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Novel insights into bacterial signalling: the one sequence-multiple structures´ perspective
Autor/es:
TRAJTENBERG, FELIPE; BOTTI, HORACIO; ALBANESI, DANIELA; DE MENDOZA, DIEGO; LARRIEUX, NICOLE; BUSCHIAZZO, ALEJANDRO
Lugar:
Puerto Varas
Reunión:
Congreso; XII PABMB Congress; 2013
Institución organizadora:
Panamerican Association for Biochemistry and Molecular Biology
Resumen:
We have focused on the study of two-component systems (TCSs), key players in bacterial signaling, to better understand signal-transmission with molecular detail. The TCS DesK/DesR controls fatty acid desaturation in Bacillus subtilis in response to cold shock and other membrane-altering effectors. We had previously put forward a model of signal-dependent allosteric control of the sensor kinase catalytic activity [1,2]. We have recently turned our attention to the response regulator DesR. A canonical activation pathway has been widely accepted to explain phosphorylation-mediated control of response regulator function, allosterically coupling the phosphorylation site to the a4ß5a5 surface. Here, using a combination of crystallography, SAXS and in vitro / in vivo functional analyses, we unveil DesR activation control by phosphorylation [3]. A novel, non-canonical route was identified, that couples phosphorylation to dimerization and cognate kinase binding.Bacterial signaling has become a good example of the 'new view' in protein structure/function principles, with 'old roots' in the MWC model of allostery and Weber's contributions to proteins' conformational equilibria. One sequence allows proteins to adopt more than one structure, and these alternate structures are frequently the basis of switching and transmission of information.[1] Albanesi et al. (2009) PNAS 106:16185[2] Trajtenberg et al. (2010) JBC 285:24892[3] Trajtenberg et al. (2013) submitted