INVESTIGADORES
GONZALEZ FLECHA Francisco Luis
congresos y reuniones científicas
Título:
Bizionia argentinensis copper chaperones
Autor/es:
NOELIA I. BURGARDT; GUSTAVO APESTEGUIA; F. LUIS GONZÁLEZ FLECHA
Lugar:
Tucuman
Reunión:
Congreso; XLI Reunion Anual de la Sociedad Argentina de Biofisica; 2012
Institución organizadora:
Sociedad Argentina de Biofisica
Resumen:
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Cellular
copper homeostasis depends of two key proteins, the CPx-type heavy
metal ATPases, which transport copper across cell membranes, and the
copper chaperones, which mediate intracellular copper transport.1
Among the copper chaperone proteins there is a group known as CopZ,
whose function is to transfer copper to CPx-type heavy metal ATPases.
The three-dimensional structure of CopZ proteins from several
organisms have been determined.2
The general fold is highly conserved and consists of a twisted
four-stranded antiparallel β-sheet and two
α-helices which are located on the same
side of the β-sheet. The metal binding
motif (MXCXXC) is found both in copper binding proteins, such as in
proteins that bind another metals.
The
genome of Bizionia argentinensis (JUB59-T), a psycrophilic
bacterium from the Antarctica sea surface, was recently reported.3
The are four open reading frames in B. argentinensis genome
with homology to CopZ. Two putative proteins (BaCopZ-33 and
BaCopZ-57), which should encoded for small proteins (13.1 and
15.5 kDa, respectively), were selected by our group. Here, we report
the cloning, expression and preliminary characterization of BaCopZ-33
and BaCopZ-57. The study of these psychrophilic proteins and
its interaction with copper would provide novel data on the mechanism
of copper binding at low temperatures and would allow a comparison
with the structures and mechanisms of analogous CopZ proteins from
mesophilic organisms.