TY - JOUR
T1 - Signal transduction by a death signal peptide
T2 - Uncovering the mechanism of bacterial killing by penicillin
AU - Novak, Rodger
AU - Charpentier, Emmanuelle
AU - Braun, Johann S.
AU - Tuomanen, Elaine
PY - 2000/1
Y1 - 2000/1
N2 - The binding of bactericidal antibiotics like penicillins, cephalosporins, and glycopeptides to their bacterial targets stops bacterial growth but does not directly cause cell death. A second process arising from the bacteria itself is necessary to trigger endogenous suicidal enzymes that dissolve the cell wall during autolysis. The signal and the trigger pathway for this event are completely unknown. Using S. pneumoniae as a model, we demonstrate that signal transduction via the two-component system VncR/S triggers multiple death pathways. We show that the signal sensed by VncR/S is a secreted peptide, Pep27, that initiates the cell death program. These data depict a novel model for the control of bacterial cell death.
AB - The binding of bactericidal antibiotics like penicillins, cephalosporins, and glycopeptides to their bacterial targets stops bacterial growth but does not directly cause cell death. A second process arising from the bacteria itself is necessary to trigger endogenous suicidal enzymes that dissolve the cell wall during autolysis. The signal and the trigger pathway for this event are completely unknown. Using S. pneumoniae as a model, we demonstrate that signal transduction via the two-component system VncR/S triggers multiple death pathways. We show that the signal sensed by VncR/S is a secreted peptide, Pep27, that initiates the cell death program. These data depict a novel model for the control of bacterial cell death.
UR - http://www.scopus.com/inward/record.url?scp=0033963751&partnerID=8YFLogxK
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U2 - 10.1016/S1097-2765(00)80402-5
DO - 10.1016/S1097-2765(00)80402-5
M3 - Article
C2 - 10678168
AN - SCOPUS:0033963751
SN - 1097-2765
VL - 5
SP - 49
EP - 57
JO - Molecular Cell
JF - Molecular Cell
IS - 1
ER -