IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Family affairs: interactions among protein phosphatases with Kelch-like domains in Arabidopsis thaliana.
Autor/es:
GUSTAVO MASELLI; RICARDO A. WOLOSIUK; SANTIAGO MORA GARCIA
Reunión:
Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular, XII PABMB Congress; 2013
Resumen:
Protein phosphatases with Kelch-like domains belong to a subfamily of the PPP Ser/Thr phosphatases, found only in green organisms and in alveolates. They are formed by three different domains: an N-terminal Kelch-like β-propeller domain, probably involved in protein-protein interactions, a C-terminal catalytic domain closely related in sequence to PP1, and an intermediate domain of unknown affiliations or functions. Arabidopsis thaliana encodes four members of the family, dubbed BSL1 to 3 and BSU1; the first three are highly conserved, whereas the latter is particularly divergent. We have previously shown that BSL2 is able to form homotypic interactions, an unusual feature in the PPP family, and described that both the catalytic and the intermediate domains are necessary. We here extend these studies to the other paralogs. We found that the behavior of some of the other members of the family characteristically differs, correlating with their phylogenetic relationships: in BSL1, the intermediate domain is dispensable, and BSU1 appears to be unable of self-interactions. Although the formation of homo- and heterotypic interactions seems to be a common feature of this family of proteins, the determinants of interaction vary.