IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Structural-functional studies of the intermediate domain of the PPKL BSL2 in Arabidopsis thaliana
Autor/es:
GUSTAVO MASELLI; SANTIAGO MORA GARCIA
Lugar:
Rosario
Reunión:
Congreso; L Reunion Anual de la Sociedad Argentina de Investigaciones Bioquimicas y de Biologia Molecular; 2014
Institución organizadora:
SAIB
Resumen:
PPKL (Protein phosphatases with Kelch-like domains) belong to a subfamily of the PPP Ser/Thr phosphatases superfamily present only in green organisms and in alveolates. They are composed by three different domains: an N-terminal Kelch-like β-propeller domain, a C-terminal catalytic domain and an intermediate domain of unknown affiliations or functions. We have previously shown that these proteins are able to form homotypic interactions, an unusual feature in the PPP family, and described that both the catalytic and/or the intermediate domains, dependig on the isoforms analyzed, are necessary and sufficient for the interaction to take place. We here report a structural-functional analysis of the 205-residue long intermediate domain of one of the paralogs in Arabidopsis thaliana, BSL2, in which this domain is necessary for the interaction. The BSL2 domain could be expressed and purified in soluble form in E.coli and behaved as a mostly intrinsically-disordered protein in solution, although it displayed a fairly high proclivity to adopt secondary-structure elements with changes in the milieu. We suggest that induced folding of (parts of) this domain upon interaction with its partner drive dimerization and possible serve other functions.