Congresos y reuniones científicas
Título:
Role of CLPLP- and SSRA- dependent proteolysis in the acidic stress-induced lysis of S. pneumoniae
Autor/es:
PIÑAS GE, ALBARRACIN ORIO AG, CORTES PR, ECHENIQUE
Reunión:
Encuentro; XLIV REUNION ANUAL SOCIEDAD ARGENTINA DE INVESTIGACION EN BIOQUIMICA Y BIOLOGIA MOLECULAR; 2008
Institución organizadora:
SAIB
Resumen:
In S. pneumoniae, we demonstrated that acidic stress triggers a
autolysin-induced lysis that is regulated by the ComE and CiaR
response regulators, which play a favoring or protective role,
respectively. We demonstrated that the ClpL ATPase, which is
highly expressed during acid exposure, is required for the acidic
stress-induced lysis (ASIL). ClpL carries out a chaperone function
and is also involved in proteolysis in association with the serine
protease ClpP. The SsrA-SmpB system mediates peptide tagging of
nascent truncated proteins, which are targeted for proteolysis via
the ClpP-chaperone complex. We constructed a clpL mutant that
showed a complete inhibition of ASIL, indicating that this
chaperone is required to fold proteins that promote ASIL. To study
the proteolysis contribution to ASIL induction, we also obtained
mutants of clpP and smpB genes. When the ASIL phenotype was
analyzed, both clpP and smpB mutants did not autolyse at acidic
pH. Considering these results, we hypothesized that acidic stressunfolded proteins are ssrA-tagged and degraded by ClpLP
complex, facilitating the ASIL process. However, we cannot
exclude the possibility that putative inhibitors of ASIL could be
degraded directly by ClpLP through the recognition of ssrA-like
tags present in their C-terminal regions, as described in E. Coli