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- W2184479124 abstract "ng proteins (PBPs) laandlb.This resistance couldbereversed bythesimultaneous addition ofmecillinam, aP-lactam thatbindsPBP2. However, eveninthepresence ofmecillinam, cells induced toproduce HSPswereresistant tolysis by ampicillin, whichbinds allthemajor PBPs.Lysis ofcells induced toproduce HSPscould also beeffected by imipenem, a(8-lactam knowntolyse nongrowing cells. Theseeffects suggest theexistence ofatleast two pathways for,-lactam-dependent lysis, oneinhibited byHSPsandonenot. HSP-mediated lysis resistance was abolished byamutation inanyoneoffive heatshockgenes (dnaK, dnaj, grpE,groES, orgroEL). Thus, resistance appeared todepend ontheexpression ofthecomplete heatshock response rather thanonanysingle HSP.Resistance tolysis wassignificant intheabsence oftheRelAprotein, implying that resistance could not beexplained byactivation ofthestringent response. Since manyenvironmental stresses promote theexpression ofHSPs,itispossible that their presence contributes anadditional mechanism toward development inbacteria ofphenotypic tolerance to(8-lactam antibiotics. Penicillin andother1-lactam derivatives bindcovalently toaspecific setofbacterial proteins, thepenicillin-bindi ng" @default.
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- W2184479124 date "1991-01-01" @default.
- W2184479124 modified "2023-09-27" @default.
- W2184479124 title "Lysis ofEscherichia coli byr-Lactams WhichBindPenicillin- Binding Proteins laandlb:Inhibition byHeatShockProteins" @default.
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- W2184479124 hasPublicationYear "1991" @default.
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