People

Jose M. Arguello

Professor

Faculty Listing
Office: Life Sciences and Bioengineering Center, 4021
Phone: +1-508-831-5326
Fax: +1-508-831-5933
arguello@wpi.edu

Related Information

Argüello Lab

Educational Background

Biological Chemist, Universidad Nacional de Córdoba - Argentina, 1979
Ph.D., Universidad Nacional de Río Cuarto - Argentina, 1985

Research & Teaching Interests

Biochemistry; biophysics; ion transport; membrane protein structure; structure-function of the Na, K-ATPase

Research

Our research goal is to understand the mechanism of ion transport by P-type ATPases. These are membrane proteins that transport cations against their concentration gradients using the energy provided by ATP hydrolysis. Studying the structure-function relationships of the Na,K-ATPase, we identified amino acids involved in cation binding and transport and the role of transmembrane segments in linking the ATP hydrolysis with conformational changes at the cation binding sites. More recently, our lab has initiated several projects to study heavy metal transport ATPases (P_IB-ATPases). These P-type ATPases transport metals (Cu⁺, Ag⁺, Zn2⁺, Co2⁺, Cd2⁺, Pb2⁺) across biomembranes and against their concentration gradients. These are key enzymes in the mechanisms of heavy metal absorption, distribution, and bioaccumulation. Using thermophilic P_IB-ATPases from extremophile archaeabacteria, we are studying the mechanisms of ion selectivity, regulation and energy transduction. In another project we are studying the physiological role of P_IB- ATPases in plant mineral metabolism. Metal micronutrients are key for plant physiology. However, little is known about the molecular mechanisms of metal transport across plant membranes. Thus, it is clear that a better knowledge of the mechanisms of metal absorption, distribution and accumulation in plants is needed for understanding and manipulating: a) plant nutrition; b) content of micronutrients required in the human diet; c) plant resistance to toxic heavy metals; and d) plant sequestration of heavy metals for phytoremediation. Genomic information from Arabidopsis thaliana shows the presence of at least six different genes encoding P_IB-ATPases. We hypothesize that the diversity of these proteins in plants implies complex roles involving differential ion specificity and expression, tissue and subcellular distribution.

Recent Publications

Sazinsky, M.H., Mandal, A.K., Argüello, J.M., and Rosenzweig, A.C. (2006) Structure of the ATP Binding Domain from the Archaeoglobus fulgidus Cu⁺-ATPase Published on line The Journal of Biological Chemistry, 281, 11161-11160
Eren, E. and Argüello, J.M. (2004) Arabidopsis HMA2, a divalent heavy metal transporting PIB-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiology 136, 3712-3723.
Mandal, A.K., Yang, Y., Kertesz, T.M., and Argüello, J.M. (2004) Identification of the transmembrane metal binding site in Cu+ transporting PIB-type ATPases. The Journal of Biological Chemistry 279, 54802-54807.
Argüello, J.M. (2003) Identification of ion selectivity determinants in heavy metal transport P1B-ATPases. The Journal of Membrane Biology, 195, 93-108.
Mandal, A.K., and Argüello, J.M. (2003) Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu⁺ ATPase CopA. Biochemistry 42, 11040-11047.

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Years of Service at WPI

Assistant Professor, WPI, 1996-2002
Associate Professor,WPI, 2002 -

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