INVESTIGADORES
BLANCATO Victor Sebastian
congresos y reuniones científicas
Título:
OadH from Enterococcus faecalis a novel subunit among the membrane-bound Oxaloacetate decarboxylases
Autor/es:
REPIZO, GD; BLANCATO, VS; MAGNI, C
Lugar:
San Miguel de Tucumán
Reunión:
Congreso; XLV Reunión Anual de SAIB; 2009
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Bilogía Molecular
Resumen:
Citrate metabolism in E.
faecalis involves
the conversion of citrate to pyruvate, by the sequential action of citrate
lyase and oxaloacetate decarboxylase (OAD) enzymes. Our previous reports
indicated that the gene cluster involved in citrate degradation in E. faecalis encodes an OAD membrane-bound
complex homologous to the one present in Klebsiella
pneumoniae. In K. pneumoniae the
complex is composed of three subunits (Kpn-α,
β and γ), while in E. faecalis a four
subunit complex was found (Ef-α, β, δ
and h). Interestingly, we found that the EfoadH gene encodes a new subunit (Ef-h), which may have functional
properties analogous to the Kpn-γ
subunit. Analysis of the subunits localization, revealed that those that
in principle were soluble (α and δ) were found in the cytoplasm as well as
attached to the membrane of E. faecalis,
suggesting that α, δ and h subunits form a soluble complex that is able to
interact with the membrane-bound β subunit in a dynamic way. In this work, the
nature of the interaction between the subunits was analyzed. We observed that
the complex was stable at acidic pH suggesting that it´s integrity could be
maintained in a different manner than the one reported for Kpn-OAD. Furthermore, different subunits were cloned and expressed
in E. coli. In summary, we propose
that the new h subunit mediates the interaction between the remaining
subunits of the complex.