IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Expression and characterization of potential Cu(I) transport ATPase from the psychrophilic bacterium Bizionia argentinensis
Autor/es:
NOELIA I. BURGARDT; F. LUIS GONZÁLEZ FLECHA
Lugar:
Chascomus
Reunión:
Congreso; IV Latin American Meeting on Biological Inorganic Chemistry; 2014
Institución organizadora:
Society of Biological Inorganic Chemistry
Resumen:
The relationships between membrane protein folding, function and stability are the main topics of research in our group1. To explore this subject we selected the PIB-ATPase family as a model. These integral membrane proteins actively transport copper through the cell membrane2. Recently, it was obtained the first crystal structure of a copper transporting PIB-ATPase (CopA) from Legionella pneumophila3 We have previously demonstrated that the thermophilic copper transporting PIB-ATPase from Archaeglobus fulgidus undergoes irreversible thermal denaturation due to a partial unfolding of the aminoacidic chain mainly at the level of the cytoplasmatic domains4. Furthermore, we found that guanidinium hydrochloride induce a reversible unfolding of CopA, allowing the complete thermodynamic characterization of the folding process5. To further explore this issue we decided to perform a comparative study of the structure-folding-function relationships in a set of copper transporting PIB-ATPases from mesophilic and psychrophilic organisms. As the psychrophilic partner we select a potential cooper transport ATPase from the recently discovered psychrophilic bacteria Bizionia argentinensis (JUB59-T), isolated from the Argentine Antarctic6,7. Here we present the cloning, expression and preliminary characterization of this psychrophilic CopA (BaCopA).