Topic
Crescentin
About: Crescentin is a research topic. Over the lifetime, 73 publications have been published within this topic receiving 12974 citations.
Papers published on a yearly basis
Papers
TL;DR: The results suggest that FtsZ self-assembles into a ring structure at the future division site and may function as a cytoskeletal element and the formation of this ring may be the point at which division is regulated.
Abstract: Genes for cell division have been identified in Escherichia coli by the isolation of conditional lethal mutations that block cell division, but do not affect DNA replication or segregation. Of these genes, ftsZ is of great interest as it acts earliest in the division pathway, is essential, its level dictates the frequency of division, and it is thought to be the target of two cell-division inhibitors, SulA, produced in response to DNA damage, and MinCD, which prevents division at old sites. Here we have used immunoelectronmicroscopy to localize the FtsZ protein to the division site. The results suggest that FtsZ self-assembles into a ring structure at the future division site and may function as a cytoskeletal element. The formation of this ring may be the point at which division is regulated.
1,520 citations
TL;DR: The distribution of the proteins in different species of bacteria, and the similarity of their sequence to eukaryotic actins, suggest that the MreB-like proteins have a cytoskeletal, actin-like role in bacterial cell morphogenesis.
976 citations
TL;DR: The crystal structure at 2.8 Å resolution of recombinant FtsZ from the hyperthermophilic methanogen Methanococcus jannaschii is reported, which shows a three-dimensional structure similar to the structure of α- and β-tubulin.
Abstract: Bacterial cell division ends with septation, the constriction of the cell wall and cell membranes that leads to the formation of two daughter cells. During septation, FtsZ, a protein of relative molecular mass 40,000 which is ubiquitous in eubacteria and is also found in archaea and chloroplasts, localizes early at the division site to form a ring-shaped septum. This septum is required for the mechanochemical process of membrane constriction. FtsZ is a GTPase with weak sequence homology to tubulins. The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules, sheets and minirings in vitro. Here we report the crystal structure at 2.8 A resolution of recombinant FtsZ from the hyperthermophilic methanogen Methanococcus jannaschii. FtsZ has two domains, one of which is a GTPase domain with a fold related to one found in the proteins p21ras and elongation factor EF-Tu. The carboxy-terminal domain, whose function is unknown, is a four-stranded beta-sheet tilted by 90 degrees against the beta-sheet of the GTPase domain. The two domains are arranged around a central helix. GDP binding is different from that typically found in GTPases and involves four phosphate-binding loops and a sugar-binding loop in the first domain, with guanine being recognized by residues in the central connecting helix. The three-dimensional structure of FtsZ is similar to the structure of alpha- and beta-tubulin.
944 citations
TL;DR: It is demonstrated that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin—the physiological polymer of eukaryotic actin, demonstrating that M reB and actin are very similar in three dimensions.
Abstract: It was thought until recently that bacteria lack the actin or tubulin filament networks that organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin-the physiological polymer of eukaryotic actin. By elucidating the MreB crystal structure we demonstrate that MreB and actin are very similar in three dimensions. Moreover, the crystals contain protofilaments, allowing visualization of actin-like strands at atomic resolution. The structure of the MreB protofilament is in remarkably good agreement with the model for F-actin, showing that the proteins assemble in identical orientations. The actin-like properties of MreB explain the finding that MreB forms large fibrous spirals under the cell membrane of rod-shaped cells, where they are involved in cell-shape determination. Thus, prokaryotes are now known to possess homologues both of tubulin, namely FtsZ, and of actin.
845 citations
TL;DR: A fluorescent derivative of the antibiotic vancomycin is used as a probe for nascent peptidoglycan synthesis in unfixed cells of various Gram-positive bacteria, providing insights into the diverse molecular strategies used by bacteria to control their cellular morphology, as well as suggesting ways in which these strategies may impact on growth rates and cell envelope structure.
805 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2019 | 1 |
| 2017 | 2 |
| 2015 | 1 |
| 2013 | 4 |
| 2012 | 4 |
| 2011 | 7 |