IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Dissecting the interaction determinants between BSL protein phosphatases
Autor/es:
GUSTAVO MASELLI; JAVIER BIANCHI; SANTIAGO MORA-GARCIA
Lugar:
Puerto Madryn, Argentina
Reunión:
Congreso; 46th Annual Meeting-Argentine Society for Biochemistry and Molecular Biology Research; 2010
Institución organizadora:
Sociedad Argentina de Investigacion en Bioquimica y Biologia Molecular
Resumen:
BSL Ser/Thr phosphatases belong to a novel family of PPP phosphatases found in all green algae, land plants and alveolates. BSL phosphatases are bimodular proteins with a b-propeller domain at the N-terminus and a conserved catalytic domain at the C-terminus. We previously reported that these proteins are able to interact with themselves, and that this interaction is common to all the members of the family in Arabidopsis and broadly dissected its requirements. We have narrowed down the region necessary for the interaction to a stretch of about 60 aminoacids in a conserved sequence outside the catalytic domain. We are currently exploring the structural features of this region. We have also shown, through different approaches, that this interaction takes place in vivo and with similar requirements. Having found that the homologs from the moss Physcomitrella patens and the unicellular green alga Chlamydomonas reinhardtii behave in a similar way, we have now extended this analysis to a model alveolate, the unicellular apicomplexan Toxoplasma gondii. The ability to interact with themselves is an unusual and novel feature among Ser/Thr phosphatases. We are presently exploring the regulatory implications on the activity.