INVESTIGADORES
GARCIA VESCOVI Eleonora
artículos
Título:
The H box-harboring domain is key to the function of the Salmonella enterica PhoQ Mg2+-sensor in the recognition of its partner PhoP
Autor/es:
CASTELLI, M. E.; CAUERHFF, A.; AMONGERO, M.; SONCINI, F. C.; GARCÍA VÉSCOVI, E.
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
American Society for Biochemistry and Molecular Biology
Referencias:
Año: 2003 vol. 278 p. 23579 - 23585
ISSN:
0021-9258
Resumen:
In two-component signaling systems, the transduction
strategy relies on a conserved His-Asp phosphoryl exchange
between the sensor histidine kinase and its cognate
response-regulator, and structural and functional
consensus motifs are found when comparing either the
diverse histidine kinases or response regulators present
in a single cell. Therefore, the mechanism that guarantees
the specific recognition between partners of an individual
pair is essential to unequivocally generate the
appropriate adaptive response. Based on sequence
alignments with other histidine kinases, we dissected
the Salmonella enterica Mg2-sensor PhoQ in different
subdomains and examined by in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows SalmonellaSalmonella
to withstand environmental Mg2 limitation by
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
2
subdomains and examined by in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows SalmonellaSalmonella
to withstand environmental Mg2 limitation by
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
2
Salmonella enterica Mg2-sensor PhoQ in different
subdomains and examined by in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
its interaction with the associated response regulator
PhoP. This signal transduction system allows Salmonella
in vivo and in vitro assays
its interaction with the associated response regulator
PhoP. This signal transduction system allows SalmonellaSalmonella
to withstand environmental Mg2 limitation by
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.
2 limitation by
triggering gene expression that is vital throughout the
infective cycle in the host. Using resonant mirror biosensor
technology, we calculated the kinetic and equilibrium
binding constants and determined that the Hisphosphotransfer
domain is essential for the PhoQ
specific recognition and interaction with PhoP. Additionally,
we show the role of this domain in the bimolecular
transphosphorylation and provide evidence that
this region undergoes dimerization.