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关键词： peptidoglycan   divisome   penicillin-binding protein 1b (PBP1b)   FtsN   lipid II   bacteria   cell division   cellular regulation   cell surface enzyme   cell wall  

摘要： Peptidoglycan (PG) is an essential constituent of the bacterial cell wall. During cell division, the machinery responsible for PG synthesis localizes mid-cell, at the septum, under the control of a multiprotein complex called the divisome. In Escherichia coli, septal PG synthesis and cell constriction rely on the accumulation of FtsN at the division site. Interestingly, a short sequence of FtsN (Leu(75)-Gln(93), known as (E)FtsN) was shown to be essential and sufficient for its functioning in vivo, but what exactly this sequence is doing remained unknown. Here, we show that (E)FtsN binds specifically to the major PG synthase PBP1b and is sufficient to stimulate its biosynthetic glycosyltransferase (GTase) activity. We also report the crystal structure of PBP1b in complex with (E)FtsN, which demonstrates that (E)FtsN binds at the junction between the GTase and UB2H domains of PBP1b. Interestingly, mutations to two residues (R141A/R397A) within the (E)FtsN-binding pocket reduced the activation of PBP1b by FtsN but not by the lipoprotein LpoB. This mutant was unable to rescue the Delta ponB-ponA(ts) strain, which lacks PBP1b and has a thermosensitive PBP1a, at nonpermissive temperature and induced a mild cell-chaining phenotype and cell lysis. Altogether, the results show that (E)FtsN interacts with PBP1b and that this interaction plays a role in the activation of its GTase activity by FtsN, which may contribute to the overall septal PG synthesis and regulation during cell division.

摘要： A recent study reports the three-dimensional structure of a primary cilium with unprecedented clarity. The results highlight the architectural differences with motile cilia and provoke a reassessment of the relationship between the ciliary cytoskeleton and microtubule-based transport in cilia.