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• W3033263072 abstract "Abstract Peptidoglycan (PG) is an essential constituent of the bacterial cell wall. During cell division PG synthesis localizes at mid-cell under the control of a multiprotein complex, the divisome. In Escherichia coli , septal PG synthesis and cell constriction rely on the accumulation of FtsN at the division site. The region L75 to Q93 of FtsN ( E FtsN) was shown to be essential and sufficient for its functioning in vivo but the specific target and the molecular mechanism remained unknown. Here, we show that E FtsN binds specifically to the major PG synthase PBP1b and is sufficient to stimulate its GTase activity. We also report the crystal structure of PBP1b in complex with E FtsN which provides structural insights into the mode of binding of E FtsN at the junction between the GTase and UB2H domains of PBP1b. Interestingly, the mutations R141A/R397A of PBP1b, within the E FtsN binding pocket, reduce the activation of PBP1b by FtsN. This mutant was unable to rescue Δ ponB - ponA ts strain at nonpermissive temperature and induced a mild cell chaining phenotype and cell lysis. Altogether, the results show that PBP1b is a target of E FtsN and suggest that binding of FtsN to PBP1b contributes to trigger septal PG synthesis and cell constriction." @default.
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• W3033263072 date "2020-06-05" @default.
• W3033263072 modified "2023-09-27" @default.
• W3033263072 title "Biochemical and structural insights into the activation of PBP1b by the essential domain of FtsN" @default.
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• W3033263072 doi "https://doi.org/10.1101/2020.06.05.136150" @default.
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