Topic
Divisome complex
About: Divisome complex is a research topic. Over the lifetime, 19 publications have been published within this topic receiving 570 citations.
Papers
TL;DR: Proteidoglycan synthesis was thought to be mediated solely by class A penicillin-binding proteins (PBPs) and related enzymes, a view changed by the identification of RodA as a PG polymerase, but now FtsW is also shown to polymerize PG, in a process that requires complex formation with its partner class B PBP.
Abstract: The peptidoglycan cell wall is essential for the survival and morphogenesis of bacteria1. For decades, it was thought that only class A penicillin-binding proteins (PBPs) and related enzymes effected peptidoglycan synthesis. Recently, it was shown that RodA-a member of the unrelated SEDS protein family-also acts as a peptidoglycan polymerase2-4. Not all bacteria require RodA for growth; however, its homologue, FtsW, is a core member of the divisome complex that appears to be universally essential for septal cell wall assembly5,6. FtsW was previously proposed to translocate the peptidoglycan precursor lipid II across the cytoplasmic membrane7,8. Here, we report that purified FtsW polymerizes lipid II into peptidoglycan, but show that its polymerase activity requires complex formation with its partner class B PBP. We further demonstrate that the polymerase activity of FtsW is required for its function in vivo. Thus, our findings establish FtsW as a peptidoglycan polymerase that works with its cognate class B PBP to produce septal peptidoglycan during cell division.
309 citations
TL;DR: A ‘forgotten’ allele of ftsL from Escherichia coli, which encodes a conserved division gene of unknown function is discovered, which promotes the premature initiation of cell division and suggests that rather than serving simply as a protein scaffold within the divisome, FtsL may play a more active role in the activation of the machine.
Abstract: The cytokinetic apparatus of bacteria is initially formed by the polymerization of the tubulin-like FtsZ protein into a ring structure at midcell. This so-called Z-ring facilitates the recruitment of many additional proteins to the division site to form the mature divisome machine. Although the assembly pathway leading to divisome formation has been well characterized, the mechanisms that trigger cell constriction remain unclear. In this report, we study a “forgotten” allele of ftsL from Escherichia coli, which encodes a conserved division gene of unknown function. We discovered that this allele promotes the premature initiation of cell division. Further analysis also revealed that the mutant bypasses the requirement for the essential division proteins ZipA, FtsK, and FtsN and partially bypasses the need for FtsA. These findings suggest that rather than serving simply as a protein scaffold within the divisome, FtsL may play a more active role in the activation of the machine. Our results support a model in which FtsL, along with its partners FtsB and FtsQ, function as part of a sensing mechanism that promotes the onset of cell wall remodeling processes needed for the initiation of cell constriction once assembly of the divisome complex is deemed complete.
146 citations
TL;DR: The present work in concert with the available in vivo data support a model in which SepF plays an important role in regulating the assembly dynamics of the divisome complex; therefore, it may have anImportant role in bacterial cell division.
101 citations
TL;DR: A review of the key protein complexes and how they are involved in cell division in pneumococcus pneumoniae is provided in this paper, where the interaction of proteins in the divisome complex that underpin the control mechanisms for cell division and cell wall synthesis and remodelling are discussed.
Abstract: Cell division in Streptococcus pneumoniae (pneumococcus) is performed and regulated by a protein complex consisting of at least 14 different protein elements; known as the divisome. Recent findings have advanced our understanding of the molecular events surrounding this process and have provided new understanding of the mechanisms that occur during the division of pneumococcus. This review will provide an overview of the key protein complexes and how they are involved in cell division. We will discuss the interaction of proteins in the divisome complex that underpin the control mechanisms for cell division and cell wall synthesis and remodelling that are required in S. pneumoniae, including the involvement of virulence factors and capsular polysaccharides.
29 citations
TL;DR: FtsW is established as a peptidoglycan polymerase that works with its cognate bPBP to produce septal peptidglycan during cell division and depends on the presence of the class B PBP that it recruits to the septum.
Abstract: The peptidoglycan cell wall is essential for the survival and shape maintenance ofbacteria.1 For decades it was thought that only penicillin-binding proteins (PBPs) effected peptidoglycan synthesis. Recently, it was shown that RodA, a member of the Rod complex involved in side wall peptidoglycan synthesis, acts as a peptidoglycan polymerase.2–4 RodA is absent or dispensable in many bacteria that contain a cell wall; however, all of these bacteria have a RodA homologue, FtsW, which is a core member of the divisome complex that is essential for septal cell wall assembly.5,6 FtsW was previously proposed flip the peptidoglycan precursor Lipid II to the peripasm,7,8 but we report here that FtsW polymerizes Lipid II. We show that FtsW polymerase activity depends on the presence of the class B PBP (bPBP) that it recruits to the septum. We also demonstrate that the polymerase activity of FtsW is required for its function in vivo. Our findings establish FtsW as a peptidoglycan polymerase that works with its cognate bPBP to produce septal peptidoglycan during cell division.
19 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 4 |
| 2020 | 1 |
| 2019 | 3 |
| 2018 | 3 |
| 2016 | 2 |
| 2015 | 2 |